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Database: UniProt
Entry: Q7VY19_BORPE
LinkDB: Q7VY19_BORPE
Original site: Q7VY19_BORPE 
ID   Q7VY19_BORPE            Unreviewed;       259 AA.
AC   Q7VY19;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 98.
DE   SubName: Full=Probable D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:CAE41834.1};
GN   Name=pbpG {ECO:0000313|EMBL:CAE41834.1};
GN   OrderedLocusNames=BP1545 {ECO:0000313|EMBL:CAE41834.1};
OS   Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257313 {ECO:0000313|EMBL:CAE41834.1, ECO:0000313|Proteomes:UP000002676};
RN   [1] {ECO:0000313|Proteomes:UP000002676}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251
RC   {ECO:0000313|Proteomes:UP000002676};
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA   Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA   Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA   Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA   Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA   Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
CC   -!- SIMILARITY: Belongs to the peptidase S11 family.
CC       {ECO:0000256|ARBA:ARBA00007164, ECO:0000256|RuleBase:RU004016}.
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DR   EMBL; BX640415; CAE41834.1; -; Genomic_DNA.
DR   RefSeq; NP_880280.1; NC_002929.2.
DR   AlphaFoldDB; Q7VY19; -.
DR   STRING; 257313.BP1545; -.
DR   MEROPS; S11.002; -.
DR   PaxDb; 257313-BP1545; -.
DR   KEGG; bpe:BP1545; -.
DR   PATRIC; fig|257313.5.peg.1657; -.
DR   eggNOG; COG1686; Bacteria.
DR   HOGENOM; CLU_027070_0_3_4; -.
DR   Proteomes; UP000002676; Chromosome.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR018044; Peptidase_S11.
DR   InterPro; IPR001967; Peptidase_S11_N.
DR   PANTHER; PTHR21581; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR21581:SF6; TRAFFICKING PROTEIN PARTICLE COMPLEX SUBUNIT 12; 1.
DR   Pfam; PF00768; Peptidase_S11; 1.
DR   PRINTS; PR00725; DADACBPTASE1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:CAE41834.1};
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW   Protease {ECO:0000313|EMBL:CAE41834.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002676};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          10..236
FT                   /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT                   N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00768"
FT   ACT_SITE        44
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   ACT_SITE        47
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   ACT_SITE        101
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   BINDING         206
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ   SEQUENCE   259 AA;  28394 MW;  C0B745A13D242C5A CRC64;
     MPPAAASPAA EAAALRSSTA YVQDLETSTV LFAKNENVVR PIASISKLMT ALVVVDANLP
     MDEMIEITDD DVDTLKHTTS RLRVGTVLSR GDMLHLALMS SENRAAHALG RNYPGGMPAF
     VAAMNAKARS LGMLNTRFVE PTGLSSENVS SPRDLARMLR AASQRPLIHR YSTDTEYEVE
     INNRTQTFRN TNLLVRKPDW DIKVSKTGFI NEAGECLVML ARINGRDMAI VLLDSQGKLS
     RIGDAVRIRR IVQNDVAML
//
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