(data stored in SCRATCH zone)

SWISSPROT: HEMW_BACSU

ID   HEMW_BACSU              Reviewed;         379 AA.
AC   P54304;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 3.
DT   11-DEC-2019, entry version 141.
DE   RecName: Full=Heme chaperone HemW;
GN   Name=hemW {ECO:0000250|UniProtKB:P52062};
GN   Synonyms=hemN {ECO:0000303|PubMed:8757728}, yqeR;
GN   OrderedLocusNames=BSU25500;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC   STRAIN=168;
RX   PubMed=8757728; DOI=10.1099/13500872-142-7-1641;
RA   Homuth G., Heinemann M., Zuber U., Schumann W.;
RT   "The genes of lepA and hemN form a bicistronic operon in Bacillus
RT   subtilis.";
RL   Microbiology 142:1641-1649(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   genes.";
RL   Microbiology 142:3103-3111(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   SEQUENCE REVISION TO 94 AND 365-379.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 328-366.
RC   STRAIN=168 / MB11;
RX   PubMed=1339421; DOI=10.1128/jb.174.10.3300-3310.1992;
RA   Wetzstein M., Voelker U., Dedio J., Loebau S., Zuber U., Schiesswohl M.,
RA   Herget C., Hecker M., Schumann W.;
RT   "Cloning, sequencing, and molecular analysis of the dnaK locus from
RT   Bacillus subtilis.";
RL   J. Bacteriol. 174:3300-3310(1992).
RN   [6]
RP   INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=168;
RX   PubMed=9371469; DOI=10.1128/jb.179.22.7181-7185.1997;
RA   Hippler B., Homuth G., Hoffmann T., Hungerer C., Schumann W., Jahn D.;
RT   "Characterization of Bacillus subtilis hemN.";
RL   J. Bacteriol. 179:7181-7185(1997).
RN   [7]
RP   INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=10498703;
RA   Homuth G., Rompf A., Schumann W., Jahn D.;
RT   "Transcriptional control of Bacillus subtilis hemN and hemZ.";
RL   J. Bacteriol. 181:5922-5929(1999).
RN   [8]
RP   CAUTION.
RC   STRAIN=168;
RA   Hauert J.;
RL   Thesis (1977), University of Geneva, Switzerland.
CC   -!- FUNCTION: Probably acts as a heme chaperone, transferring heme to an
CC       unknown acceptor. Binds one molecule of heme per monomer, possibly
CC       covalently (By similarity). Binds 1 [4Fe-4S] cluster. The cluster is
CC       coordinated with 3 cysteines and an exchangeable S-adenosyl-L-
CC       methionine (By similarity). {ECO:0000250|UniProtKB:P32131,
CC       ECO:0000250|UniProtKB:P52062}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9CGF7}.
CC   -!- INDUCTION: Part of the lepA-hemN operon; there is a strong
CC       transcriptional terminator between the 2 genes, this gene is much less
CC       transcribed. There can be further readthough downstream
CC       (PubMed:8757728, PubMed:9371469). Induced under anaerobic conditions by
CC       resDE, fnr and arfM. {ECO:0000269|PubMed:10498703,
CC       ECO:0000269|PubMed:8757728, ECO:0000269|PubMed:9371469}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene accumulate
CC       coproporphyrinogen-III under anaerobic conditions, but show normal
CC       growth under aerobic and anaerobic conditions.
CC       {ECO:0000269|PubMed:10498703, ECO:0000269|PubMed:9371469}.
CC   -!- MISCELLANEOUS: Might carry two S-adenosyl-L-methionine binding sites
CC       with only one binding to the iron-sulfur cluster.
CC       {ECO:0000250|UniProtKB:P32131}.
CC   -!- SIMILARITY: Belongs to the anaerobic coproporphyrinogen-III oxidase
CC       family. HemW subfamily. {ECO:0000305}.
CC   -!- CAUTION: Although the bacteria accumulates coproporphyrinogen-III when
CC       the gene is disrupted, no oxygen-independent coproporphyrinogen-III
CC       oxidase activity or complementation have been shown. The exact role of
CC       this protein is unknown. {ECO:0000305|PubMed:10498703,
CC       ECO:0000305|PubMed:9371469}.
DR   EMBL; X91655; CAB61616.1; -; Genomic_DNA.
DR   EMBL; D84432; BAA12461.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14492.2; -; Genomic_DNA.
DR   EMBL; M84964; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; B69640; B69640.
DR   RefSeq; NP_390428.2; NC_000964.3.
DR   RefSeq; WP_004398764.1; NZ_JNCM01000036.1.
DR   SMR; P54304; -.
DR   STRING; 224308.BSU25500; -.
DR   PaxDb; P54304; -.
DR   PRIDE; P54304; -.
DR   EnsemblBacteria; CAB14492; CAB14492; BSU25500.
DR   GeneID; 937845; -.
DR   KEGG; bsu:BSU25500; -.
DR   PATRIC; fig|224308.179.peg.2771; -.
DR   eggNOG; ENOG4105CSA; Bacteria.
DR   eggNOG; COG0635; LUCA.
DR   HOGENOM; HOG000015380; -.
DR   InParanoid; P54304; -.
DR   KO; K02495; -.
DR   OMA; GPSAHSF; -.
DR   PhylomeDB; P54304; -.
DR   BioCyc; BSUB:BSU25500-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; ISS:UniProtKB.
DR   GO; GO:0004109; F:coproporphyrinogen oxidase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IMP:UniProtKB.
DR   Gene3D; 3.80.30.20; -; 1.
DR   InterPro; IPR034505; Coproporphyrinogen-III_oxidase.
DR   InterPro; IPR006638; Elp3/MiaB/NifB.
DR   InterPro; IPR010723; HemN_C.
DR   InterPro; IPR004559; HemW-like.
DR   InterPro; IPR007197; rSAM.
DR   InterPro; IPR023404; rSAM_horseshoe.
DR   PANTHER; PTHR13932; PTHR13932; 1.
DR   Pfam; PF06969; HemN_C; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   SMART; SM00729; Elp3; 1.
DR   TIGRFAMs; TIGR00539; hemN_rel; 1.
PE   2: Evidence at transcript level;
DR   PRODOM; P54304.
DR   SWISS-2DPAGE; P54304.
KW   4Fe-4S; Chaperone; Cytoplasm; Heme; Iron; Iron-sulfur; Metal-binding;
KW   Reference proteome; S-adenosyl-L-methionine.
FT   CHAIN           1..379
FT                   /note="Heme chaperone HemW"
FT                   /id="PRO_0000109939"
FT   REGION          61..62
FT                   /note="S-adenosyl-L-methionine 2 binding"
FT                   /evidence="ECO:0000250|UniProtKB:P32131"
FT   METAL           11
FT                   /note="Iron-sulfur (4Fe-4S-S-AdoMet)"
FT                   /evidence="ECO:0000250|UniProtKB:P32131"
FT   METAL           15
FT                   /note="Iron-sulfur (4Fe-4S-S-AdoMet)"
FT                   /evidence="ECO:0000250|UniProtKB:P32131"
FT   METAL           18
FT                   /note="Iron-sulfur (4Fe-4S-S-AdoMet)"
FT                   /evidence="ECO:0000250|UniProtKB:P32131"
FT   BINDING         5
FT                   /note="S-adenosyl-L-methionine 1"
FT                   /evidence="ECO:0000250|UniProtKB:P32131"
FT   BINDING         60
FT                   /note="S-adenosyl-L-methionine 1; via amide nitrogen and
FT                   carbonyl oxygen"
FT                   /evidence="ECO:0000250|UniProtKB:P32131"
FT   BINDING         94
FT                   /note="S-adenosyl-L-methionine 1"
FT                   /evidence="ECO:0000250|UniProtKB:P32131"
FT   BINDING         121
FT                   /note="S-adenosyl-L-methionine 2"
FT                   /evidence="ECO:0000250|UniProtKB:P32131"
FT   BINDING         133
FT                   /note="S-adenosyl-L-methionine 2"
FT                   /evidence="ECO:0000250|UniProtKB:P32131"
FT   BINDING         158
FT                   /note="S-adenosyl-L-methionine 2"
FT                   /evidence="ECO:0000250|UniProtKB:P32131"
FT   CONFLICT        94
FT                   /note="E -> D (in Ref. 2; BAA12461)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        175
FT                   /note="I -> S (in Ref. 1; CAB61616)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        365..379
FT                   /note="KLLGNEVFGAFLGEL -> NY (in Ref. 1; CAB61616, 2;
FT                   BAA12461 and 5; M84964)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   379 AA;  42888 MW;  ECEC9FC2D638D3FF CRC64;
     MKSAYIHIPF CEHICHYCDF NKYFIQSQPV DEYLNALEQE MINTIAKTGQ PDLKTIFIGG
     GTPTSLSEEQ LKKLMDMINR VLKPSSDLSE FAVEANPDDL SAEKLKILKE AGVNRLSFGV
     QTFEDDLLEK IGRVHKQKDV FTSFERAREI GFENISLDLM FGLPGQTLKH LEHSINTALS
     LDAEHYSVYS LIVEPKTVFY NLMQKGRLHL PPQEQEAEMY EIVMSKMEAH GIHQYEISNF
     AKAGMESKHN LTYWSNEQYF GFGAGAHGYI GGTRTVNVGP VKHYIDLIAE KGFPYRDTHE
     VTTEEQIEEE MFLGLRKTAG VSKKRFAEKY GRSLDGLFPS VLKDLAEKGL IHNSESAVYL
     THQGKLLGNE VFGAFLGEL
//

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