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Database: UniProt
Entry: A0A0A7KAN4_9FLAO
LinkDB: A0A0A7KAN4_9FLAO
Original site: A0A0A7KAN4_9FLAO 
ID   A0A0A7KAN4_9FLAO        Unreviewed;       245 AA.
AC   A0A0A7KAN4;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:AIZ41648.1};
GN   ORFNames=M666_08700 {ECO:0000313|EMBL:AIZ41648.1};
OS   Cellulophaga baltica 18.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Cellulophaga.
OX   NCBI_TaxID=1348584 {ECO:0000313|EMBL:AIZ41648.1, ECO:0000313|Proteomes:UP000030786};
RN   [1] {ECO:0000313|EMBL:AIZ41648.1, ECO:0000313|Proteomes:UP000030786}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=18 {ECO:0000313|EMBL:AIZ41648.1,
RC   ECO:0000313|Proteomes:UP000030786};
RX   PubMed=24428166; DOI=10.1111/1462-2920.12391;
RA   Holmfeldt K., Howard-Varona C., Solonenko N., Sullivan M.B.;
RT   "Contrasting genomic patterns and infection strategies of two co-existing
RT   Bacteroidetes podovirus genera.";
RL   Environ. Microbiol. 16:2501-2513(2014).
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DR   EMBL; CP009976; AIZ41648.1; -; Genomic_DNA.
DR   RefSeq; WP_029447018.1; NZ_CP009976.1.
DR   AlphaFoldDB; A0A0A7KAN4; -.
DR   STRING; 1348584.M666_08700; -.
DR   GeneID; 78060815; -.
DR   KEGG; cbat:M666_08700; -.
DR   HOGENOM; CLU_081855_0_0_10; -.
DR   OrthoDB; 9792074at2; -.
DR   Proteomes; UP000030786; Chromosome.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd14847; DD-carboxypeptidase_like; 1.
DR   Gene3D; 3.30.1380.10; -; 1.
DR   InterPro; IPR009045; Hedgehog_sig/DD-Pept_Zn-bd_sf.
DR   InterPro; IPR003709; Pept_M15B.
DR   PANTHER; PTHR34385; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR34385:SF1; PEPTIDOGLYCAN L-ALANYL-D-GLUTAMATE ENDOPEPTIDASE CWLK; 1.
DR   Pfam; PF02557; VanY; 1.
DR   SUPFAM; SSF55166; Hedgehog/DD-peptidase; 1.
PE   4: Predicted;
KW   Carboxypeptidase {ECO:0000313|EMBL:AIZ41648.1};
KW   Hydrolase {ECO:0000313|EMBL:AIZ41648.1};
KW   Protease {ECO:0000313|EMBL:AIZ41648.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..245
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002041743"
FT   DOMAIN          51..195
FT                   /note="Peptidase M15B"
FT                   /evidence="ECO:0000259|Pfam:PF02557"
SQ   SEQUENCE   245 AA;  28135 MW;  28A534D65BC5ED1D CRC64;
     MQRRSFIKKT TASGLALALA PSITFAQDKD VEYSILELMG KSDVKLYGKG INLRKEAHDA
     FIEMKRAAYT GGIDLKIVSS YRSFDRQQVI FENKFIKYTD AGMAPLDAIS KIIEYSTIPG
     TSRHHWGTDI DVIDGYQKVS GDVLVPSKYG EGQPFADFKK WMDENSEKFG FYLVYTDDKK
     RRGFKYEPWH YSYAPISIPM LETFRSKNLL QIYKDEDFLG SEHFTSGFLR TYITDNVLDI
     NSKLL
//
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