ID A8T6M8_9VIBR Unreviewed; 484 AA.
AC A8T6M8;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 13-SEP-2023, entry version 48.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase/D-alanyl-D-alanine-endopeptidase {ECO:0000313|EMBL:EDP58635.1};
GN ORFNames=AND4_14391 {ECO:0000313|EMBL:EDP58635.1};
OS Vibrio sp. AND4.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=314289 {ECO:0000313|EMBL:EDP58635.1, ECO:0000313|Proteomes:UP000005159};
RN [1] {ECO:0000313|EMBL:EDP58635.1, ECO:0000313|Proteomes:UP000005159}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AND4 {ECO:0000313|EMBL:EDP58635.1,
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 -!- SIMILARITY: Belongs to the peptidase S13 family.
CC {ECO:0000256|ARBA:ARBA00006096}.
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:EDP58635.1}.
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DR EMBL; ABGR01000008; EDP58635.1; -; Genomic_DNA.
DR AlphaFoldDB; A8T6M8; -.
DR MEROPS; S13.001; -.
DR Proteomes; UP000005159; Unassembled WGS sequence.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.50.80.20; D-Ala-D-Ala carboxypeptidase C, peptidase S13; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR000667; Peptidase_S13.
DR NCBIfam; TIGR00666; PBP4; 1.
DR PANTHER; PTHR30023; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR30023:SF0; PENICILLIN-SENSITIVE CARBOXYPEPTIDASE A; 1.
DR Pfam; PF02113; Peptidase_S13; 1.
DR PRINTS; PR00922; DADACBPTASE3.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:EDP58635.1};
KW Hydrolase {ECO:0000313|EMBL:EDP58635.1};
KW Protease {ECO:0000313|EMBL:EDP58635.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..484
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002727118"
SQ SEQUENCE 484 AA; 53717 MW; 44B9312D406F005B CRC64;
MRLRCSLLLF FSLAPFASMA DLHQEAYPHQ ELLPQGSRIS LIAEKLNDQS ELTSIQPTDQ
YFPPASTLKV ITALAAKLEL GNNFAFRTTL ESSSSDAVLT FSGDPTLLTQ DLKAMLTRAK
KNGFDKIKGN LWLDNSAFTG YNRAVGWPWD ILGVCYSAPA SAITLNDNCV QASIYTKKNG
TTRVYVPEHQ PIKVKTNVQT VSKSVQKSRH CNLDLIANPD NTYQLTGCLV DRGDKPLPLK
FAVQDPEHYT SQKVQKLLKQ VGISLKGNVR IGKAPEKQRK LLAIHKSKPL PQLLDQMLKH
SDNLIADTLT KTLGAKFFIQ PGSFTNGTEA IKQIILANTG VDIRDARLED GSGLSRNNRI
SAPAMAAILR YIWRHENELG LIAIMPKSGV SGTLQYRRSM RKAPIKGQLI AKSGSLYGTY
NMAGYGLDKN GKPNTVFVQF VSDYFPEKRD DNKPAVPPIT QFEKQFYQDI VNFSQATPKK
TPKK
//
