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Database: UniProt
Entry: B0VTR5_ACIBS
LinkDB: B0VTR5_ACIBS
Original site: B0VTR5_ACIBS 
ID   B0VTR5_ACIBS            Unreviewed;       439 AA.
AC   B0VTR5;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   24-JAN-2024, entry version 89.
DE   SubName: Full=D-ala-D-ala-carboxypeptidase, penicillin-binding protein {ECO:0000313|EMBL:CAP00352.1};
DE            EC=3.4.16.4 {ECO:0000313|EMBL:CAP00352.1};
GN   OrderedLocusNames=ABSDF0993 {ECO:0000313|EMBL:CAP00352.1};
OS   Acinetobacter baumannii (strain SDF).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=509170 {ECO:0000313|EMBL:CAP00352.1, ECO:0000313|Proteomes:UP000001741};
RN   [1] {ECO:0000313|EMBL:CAP00352.1, ECO:0000313|Proteomes:UP000001741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SDF {ECO:0000313|EMBL:CAP00352.1,
RC   ECO:0000313|Proteomes:UP000001741};
RX   PubMed=18350144; DOI=10.1371/journal.pone.0001805;
RA   Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E.,
RA   Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J.,
RA   Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C.,
RA   Weissenbach J., Cruveiller S.;
RT   "Comparative analysis of Acinetobacters: three genomes for three
RT   lifestyles.";
RL   PLoS ONE 3:E1805-E1805(2008).
CC   -!- SIMILARITY: Belongs to the peptidase S11 family.
CC       {ECO:0000256|ARBA:ARBA00007164, ECO:0000256|RuleBase:RU004016}.
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DR   EMBL; CU468230; CAP00352.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0VTR5; -.
DR   KEGG; abm:ABSDF0993; -.
DR   HOGENOM; CLU_027070_8_1_6; -.
DR   OMA; WQIIYNI; -.
DR   BioCyc; ABAU509170:GCL9-799-MONOMER; -.
DR   Proteomes; UP000001741; Chromosome.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
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:CAP00352.1};
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CAP00352.1};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW   Protease {ECO:0000313|EMBL:CAP00352.1};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..439
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002758546"
FT   DOMAIN          28..241
FT                   /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT                   N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00768"
FT   ACT_SITE        60
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   ACT_SITE        63
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   ACT_SITE        122
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT   BINDING         224
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ   SEQUENCE   439 AA;  48899 MW;  648992DE038750C0 CRC64;
     MKFFLSLFTL FSIFCTTLTN AALLNIAPES VEAAAWTIVD TQSGQIIAEH NSHVQRAPAS
     LTKMMVAYIA LKEIKAGKLK LNEVITATPV VSVVQWDESQ MYLKAGEQIS VDQLLAGLIV
     MSANDAAVTL AEKISGDVPH FVQRMNQEAQ ALGMKDTHFS NPAGITMPDH YTTAHDLSLL
     SQAVIHQTPE YLHYSKMPSF SYNQRFHHAT NLALKYDPSV DGLKTGYTQA AGYNLALTAS
     RPSFSPNLPQ RRLLVIVLGT PSAVKRAEIA DKLMNLAYAY TRDEVVIPEQ KLIAELPVIK
     STLKMFKVET KQPTIVTTSL YAEPTPIDLN TFDYATQRIQ VLDSNQQPKV IAPLETTQTR
     VNIQLNEQKL TAPLMKAMNL ATVSIYQNNQ LIRSLQIEND VHIEEANIFQ RIMMWFSNLF
     SIFSSSEHSA AKLYPIDSH
//
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