(data stored in SCRATCH zone)

SWISSPROT: YCIB_BACSU

ID   YCIB_BACSU              Reviewed;         194 AA.
AC   C0SP99; P94399; Q797Q0;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   11-DEC-2019, entry version 54.
DE   RecName: Full=Putative L,D-transpeptidase YciB;
DE            EC=2.-.-.-;
DE   Flags: Precursor;
GN   Name=yciB; OrderedLocusNames=BSU03350;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8969502; DOI=10.1099/13500872-142-11-3047;
RA   Yamane K., Kumano M., Kurita K.;
RT   "The 25 degrees-36 degrees region of the Bacillus subtilis chromosome:
RT   determination of the sequence of a 146 kb segment and identification of 113
RT   genes.";
RL   Microbiology 142:3047-3056(1996).
RN   [2]
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   [3]
RP   SEQUENCE REVISION TO 166.
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   [4]
RP   INDUCTION.
RC   STRAIN=168 / CU1065;
RX   PubMed=12426338; DOI=10.1128/jb.184.23.6508-6514.2002;
RA   Gaballa A., Wang T., Ye R.W., Helmann J.D.;
RT   "Functional analysis of the Bacillus subtilis Zur regulon.";
RL   J. Bacteriol. 184:6508-6514(2002).
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC   -!- INDUCTION: Repressed by zinc via the metallo-regulatory protein zur.
CC       {ECO:0000269|PubMed:12426338}.
CC   -!- SIMILARITY: Belongs to the YkuD family. {ECO:0000305}.
DR   EMBL; D50453; BAA08969.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12129.2; -; Genomic_DNA.
DR   PIR; A69760; A69760.
DR   RefSeq; NP_388217.2; NC_000964.3.
DR   RefSeq; WP_003246380.1; NZ_JNCM01000030.1.
DR   SMR; C0SP99; -.
DR   STRING; 224308.BSU03350; -.
DR   TCDB; 9.B.10.1.1; the putative tripartite zn(2+) transporter (tzt) family.
DR   PaxDb; C0SP99; -.
DR   PRIDE; C0SP99; -.
DR   EnsemblBacteria; CAB12129; CAB12129; BSU03350.
DR   GeneID; 938318; -.
DR   KEGG; bsu:BSU03350; -.
DR   PATRIC; fig|224308.179.peg.349; -.
DR   eggNOG; ENOG4105S7A; Bacteria.
DR   eggNOG; COG1376; LUCA.
DR   HOGENOM; HOG000288930; -.
DR   InParanoid; C0SP99; -.
DR   OMA; KMESKEP; -.
DR   PhylomeDB; C0SP99; -.
DR   BioCyc; BSUB:BSU03350-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0071972; F:peptidoglycan L,D-transpeptidase activity; IBA:GO_Central.
DR   GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0018104; P:peptidoglycan-protein cross-linking; IBA:GO_Central.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.440.10; -; 1.
DR   InterPro; IPR005490; LD_TPept_cat_dom.
DR   InterPro; IPR038063; Transpep_catalytic_dom.
DR   Pfam; PF03734; YkuD; 1.
DR   SUPFAM; SSF141523; SSF141523; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   2: Evidence at transcript level;
DR   PRODOM; C0SP99.
DR   SWISS-2DPAGE; C0SP99.
KW   Cell membrane; Cell shape; Cell wall biogenesis/degradation;
KW   Glycosyltransferase; Hydrolase; Lipoprotein; Membrane; Palmitate;
KW   Peptidoglycan synthesis; Reference proteome; Signal; Transferase.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           20..194
FT                   /note="Putative L,D-transpeptidase YciB"
FT                   /id="PRO_0000387934"
FT   LIPID           20
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           20
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CONFLICT        166
FT                   /note="A -> V (in Ref. 1; BAA08969)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   194 AA;  22054 MW;  25DFFF1A82E70D5E CRC64;
     MKLSLFIIAV LMPVILLSAC SDHAEEHASI NTKKTVENIT DVRKTAKTSI DWTKPSGGEY
     PDIKQKHVWI DVNVKEQKAY IKEGSNTIYT MMISSGLDQT KDDATPKGTF YVEPERGEWF
     FSEGYQEGAE YWVSWKNHGE FLFHSVPMTK DQKVIKTEAE KLGTKASHGC IRLTIPDAKW
     VYENIPEHTK VVIS
//

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