ID A0A0L0LCR9_9BACT Unreviewed; 297 AA.
AC A0A0L0LCR9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 22-FEB-2023, entry version 16.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:KND47838.1};
DE EC=3.4.16.4 {ECO:0000313|EMBL:KND47838.1};
GN ORFNames=AB201_02915 {ECO:0000313|EMBL:KND47838.1};
OS Parcubacteria bacterium C7867-006.
OC Bacteria; Candidatus Parcubacteria.
OX NCBI_TaxID=1659200 {ECO:0000313|EMBL:KND47838.1, ECO:0000313|Proteomes:UP000037457};
RN [1] {ECO:0000313|EMBL:KND47838.1, ECO:0000313|Proteomes:UP000037457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C7867-006 {ECO:0000313|EMBL:KND47838.1};
RX PubMed=26257709; DOI=10.3389/fmicb.2015.00713;
RA Nelson W.C., Stegen J.C.;
RT "The reduced genomes of Parcubacteria (OD1) contain signatures of a
RT symbiotic lifestyle.";
RL Front. Microbiol. 6:713-713(2015).
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:KND47838.1}.
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DR EMBL; LFCP01000003; KND47838.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L0LCR9; -.
DR STRING; 1659200.AB201_02915; -.
DR PATRIC; fig|1659200.3.peg.495; -.
DR Proteomes; UP000037457; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd14852; LD-carboxypeptidase; 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:KND47838.1};
KW Hydrolase {ECO:0000313|EMBL:KND47838.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:KND47838.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 147..266
FT /note="Peptidase M15B"
FT /evidence="ECO:0000259|Pfam:PF02557"
SQ SEQUENCE 297 AA; 34217 MW; 95654AEFFAEAEBC9 CRC64;
MKEKIKKLMP DKVILSACIA LILTSFIYDG YIFYKMRDLN ISLENQVATY KQALSITQNN
LFKVRGEKDA ILTILGAERQ NNSYIQSQIQ DITSTVGQLQ KLSQTDVELL KKYSKVYFLN
ENYVPPRLSA IEDRYLNIKN KPLEILSDIY PKLKLMLDDA KAQGVDIQIL SAYRSFSTQA
GLKSAYKVTY GYGANKFSAD QGYSEHQLGT TIDFTTPKIG SVLTGFEKTD AYKWLTANAY
KYGFILSYPK NNTYYIYEPW HWRFVGVTLA TRLHDQNLNF YDVSQRDIDQ YLANIFD
//
