(data stored in SCRATCH zone)

SWISSPROT: APBC_BACSU

ID   APBC_BACSU              Reviewed;         352 AA.
AC   P50863;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   11-DEC-2019, entry version 120.
DE   RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000255|HAMAP-Rule:MF_02040};
GN   Name=salA; Synonyms=mrp, rec233, ybaL, ybxI; OrderedLocusNames=BSU01540;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7559346; DOI=10.1128/jb.177.19.5582-5589.1995;
RA   Sekiguchi J., Akeo K., Yamamoto H., Khasanov F.K., Alonso J.C., Kuroda A.;
RT   "Nucleotide sequence and regulation of a new putative cell wall hydrolase
RT   gene, cwlD, which affects germination in Bacillus subtilis.";
RL   J. Bacteriol. 177:5582-5589(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8969501; DOI=10.1099/13500872-142-11-3039;
RA   Yasumoto K., Liu H., Jeong S.M., Ohashi Y., Kakinuma S., Tanaka K.,
RA   Kawamura F., Yoshikawa H., Takahashi H.;
RT   "Sequence analysis of a 50 kb region between spo0H and rrnH on the Bacillus
RT   subtilis chromosome.";
RL   Microbiology 142:3039-3046(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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 328-352.
RC   STRAIN=168;
RX   PubMed=2517635; DOI=10.1099/00221287-135-12-3431;
RA   Yon J.R., Sammons R.L., Smith D.A.;
RT   "Cloning and sequencing of the gerD gene of Bacillus subtilis.";
RL   J. Gen. Microbiol. 135:3431-3445(1989).
RN   [5]
RP   FUNCTION.
RX   PubMed=15126467; DOI=10.1128/jb.186.10.3056-3064.2004;
RA   Ogura M., Matsuzawa A., Yoshikawa H., Tanaka T.;
RT   "Bacillus subtilis SalA (YbaL) negatively regulates expression of scoC,
RT   which encodes the repressor for the alkaline exoprotease gene, aprE.";
RL   J. Bacteriol. 186:3056-3064(2004).
CC   -!- FUNCTION: Binds and transfers iron-sulfur (Fe-S) clusters to target
CC       apoproteins. Can hydrolyze ATP. {ECO:0000255|HAMAP-Rule:MF_02040}.
CC   -!- FUNCTION: Negatively regulates the expression of hpr/scoC. The effect
CC       on hpr/scoC may be indirect. {ECO:0000269|PubMed:15126467}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02040}.
CC   -!- INDUCTION: Autoregulated.
CC   -!- SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family.
CC       {ECO:0000255|HAMAP-Rule:MF_02040}.
DR   EMBL; X74737; CAA52756.1; -; Genomic_DNA.
DR   EMBL; D64126; BAA10994.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11930.1; -; Genomic_DNA.
DR   EMBL; M27259; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; A69743; A69743.
DR   RefSeq; NP_388035.1; NC_000964.3.
DR   RefSeq; WP_003235124.1; NZ_JNCM01000029.1.
DR   IntAct; P50863; 5.
DR   MINT; P50863; -.
DR   STRING; 224308.BSU01540; -.
DR   jPOST; P50863; -.
DR   PaxDb; P50863; -.
DR   PRIDE; P50863; -.
DR   EnsemblBacteria; CAB11930; CAB11930; BSU01540.
DR   GeneID; 938914; -.
DR   KEGG; bsu:BSU01540; -.
DR   PATRIC; fig|224308.179.peg.158; -.
DR   eggNOG; ENOG4105D1F; Bacteria.
DR   eggNOG; COG0489; LUCA.
DR   HOGENOM; HOG000079915; -.
DR   InParanoid; P50863; -.
DR   KO; K03593; -.
DR   OMA; PHATAAF; -.
DR   PhylomeDB; P50863; -.
DR   BioCyc; BSUB:BSU01540-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; IBA:GO_Central.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:CACAO.
DR   HAMAP; MF_02040; Mrp_NBP35; 1.
DR   InterPro; IPR019591; Mrp/NBP35_ATP-bd.
DR   InterPro; IPR000808; Mrp_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR033756; YlxH/NBP35.
DR   Pfam; PF10609; ParA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS01215; MRP; 1.
PE   2: Evidence at transcript level;
DR   PRODOM; P50863.
DR   SWISS-2DPAGE; P50863.
KW   ATP-binding; Hydrolase; Iron; Iron-sulfur; Metal-binding;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..352
FT                   /note="Iron-sulfur cluster carrier protein"
FT                   /id="PRO_0000184929"
FT   NP_BIND         114..121
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02040"
FT   CONFLICT        328
FT                   /note="D -> Y (in Ref. 4)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   352 AA;  38639 MW;  255633623E8623DB CRC64;
     MIREDEVRKL VGEMREPFLQ RPLGELDAVK EIKIKPEKRH ISVKVALAKT GTAEQMQIQQ
     EIVNVLKGAG AETVGLRFEE LPEETVAKFR APSAEKKTLL NMDNPPVFLA VASGKGGVGK
     STVSVNLAIS LARLGKKVGL IDADIYGFSV PDMMGITVRP TIEGEKLLPV ERFGVKVMSM
     GFFVEENAPV VWRGPMLGKM LNNFFHEVEW GEVDYIVLDL PPGTGDVALD VHTMLPSCKE
     IIVSTPHPTA AFVAARAGSM AIKTDHEVVG VIENMAYYES AKTGEREYVF GKGGGDKLAE
     ELNVPLLGRI PLKQPDWDKD QFAPSVYDEN HPIGEIYQDI AKKIDAKMSV QV
//

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