ID A8T3B3_9VIBR Unreviewed; 388 AA.
AC A8T3B3;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=serine-type D-Ala-D-Ala carboxypeptidase {ECO:0000256|ARBA:ARBA00012448};
DE EC=3.4.16.4 {ECO:0000256|ARBA:ARBA00012448};
GN ORFNames=AND4_10944 {ECO:0000313|EMBL:EDP59669.1};
OS Vibrio sp. AND4.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=314289 {ECO:0000313|EMBL:EDP59669.1, ECO:0000313|Proteomes:UP000005159};
RN [1] {ECO:0000313|EMBL:EDP59669.1, ECO:0000313|Proteomes:UP000005159}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AND4 {ECO:0000313|EMBL:EDP59669.1,
RC ECO:0000313|Proteomes:UP000005159};
RX PubMed=20436956; DOI=10.1371/journal.pbio.1000358;
RA Gomez-Consarnau L., Akram N., Lindell K., Pedersen A., Neutze R.,
RA Milton D.L., Gonzalez J.M., Pinhassi J.;
RT "Proteorhodopsin phototrophy promotes survival of marine bacteria during
RT starvation.";
RL PLoS Biol. 8:E1000358-E1000358(2010).
CC -!- FUNCTION: Removes C-terminal D-alanyl residues from sugar-peptide cell
CC wall precursors. {ECO:0000256|ARBA:ARBA00003217}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also
CC transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC substituents of D-alanine.; EC=3.4.16.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034000};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
CC -!- SIMILARITY: Belongs to the peptidase S11 family.
CC {ECO:0000256|ARBA:ARBA00007164, ECO:0000256|RuleBase:RU004016}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EDP59669.1}.
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DR EMBL; ABGR01000003; EDP59669.1; -; Genomic_DNA.
DR RefSeq; WP_009842063.1; NZ_ABGR01000003.1.
DR AlphaFoldDB; A8T3B3; -.
DR OrthoDB; 9795979at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000005159; Unassembled WGS sequence.
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-UniPathway.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 2.60.410.10; D-Ala-D-Ala carboxypeptidase, C-terminal domain; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR015956; Peniciliin-bd_prot_C_sf.
DR InterPro; IPR018044; Peptidase_S11.
DR InterPro; IPR012907; Peptidase_S11_C.
DR InterPro; IPR037167; Peptidase_S11_C_sf.
DR InterPro; IPR001967; Peptidase_S11_N.
DR PANTHER; PTHR21581; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR21581:SF34; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACC; 1.
DR Pfam; PF07943; PBP5_C; 1.
DR Pfam; PF00768; Peptidase_S11; 1.
DR PRINTS; PR00725; DADACBPTASE1.
DR SMART; SM00936; PBP5_C; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF69189; Penicillin-binding protein associated domain; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW ECO:0000313|EMBL:EDP59669.1}; 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:0000256|ARBA:ARBA00022670};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..388
FT /note="serine-type D-Ala-D-Ala carboxypeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002729972"
FT DOMAIN 278..368
FT /note="Peptidase S11 D-Ala-D-Ala carboxypeptidase A C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00936"
FT ACT_SITE 62
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 65
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 125
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 228
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 388 AA; 42309 MW; 76F82053D404CCD0 CRC64;
MNTLRTRFTF VCLLLASSCL PALAVVTPNP PQLQAKGYVL MDFQSGAIIA EQNARAGLAP
ASLTKLMTAY VVGQEIKSGR LQWDDKVTVS ENAWSAKFPD SSKMFIQPND EITIANLMRG
VIIQSGNDAC VALAEHVAGS EGAFVSLMNG WADKLSLNDT YFVNSHGLDS EGIQTSPNDM
ATLMQAIIND VPEVYALYSE KVFKWNKITQ YNRNKLLWDK SMDVDGGKTG YTSNAGYSLV
SSAKQGKMRL ISVVMGTPSK QSRITQSKNL LSYGFRFYGT KQVAKQGEVQ ASAKVWKGDV
SKIDLGFAQD AYLTLPRSLT AGLDKSAVVN EPLIAPIAKG DVVGKVVWKN DGQTVASYPL
VSYQAVEEGS WIGQLWDSLV LWVKSLFD
//
