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
//