ID A0A0A2T9L3_9BACI Unreviewed; 303 AA.
AC A0A0A2T9L3;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:KGP72234.1};
GN ORFNames=N782_13320 {ECO:0000313|EMBL:KGP72234.1};
OS Pontibacillus yanchengensis Y32.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Pontibacillus.
OX NCBI_TaxID=1385514 {ECO:0000313|EMBL:KGP72234.1, ECO:0000313|Proteomes:UP000030147};
RN [1] {ECO:0000313|EMBL:KGP72234.1, ECO:0000313|Proteomes:UP000030147}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y32 {ECO:0000313|EMBL:KGP72234.1,
RC ECO:0000313|Proteomes:UP000030147};
RX PubMed=26561516; DOI=10.1186/s40793-015-0085-y;
RA Huang J., Qiao Z.X., Tang J.W., Wang G.;
RT "High quality draft genome sequence of the moderately halophilic bacterium
RT Pontibacillus yanchengensis Y32(T) and comparison among Pontibacillus
RT genomes.";
RL Stand. Genomic Sci. 10:93-93(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:KGP72234.1}.
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DR EMBL; AVBF01000034; KGP72234.1; -; Genomic_DNA.
DR RefSeq; WP_036820450.1; NZ_AVBF01000034.1.
DR AlphaFoldDB; A0A0A2T9L3; -.
DR STRING; 1385514.N782_13320; -.
DR eggNOG; COG1876; Bacteria.
DR OrthoDB; 9792074at2; -.
DR Proteomes; UP000030147; Unassembled WGS sequence.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
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:KGP72234.1};
KW Hydrolase {ECO:0000313|EMBL:KGP72234.1};
KW Protease {ECO:0000313|EMBL:KGP72234.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030147};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..303
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001993931"
FT DOMAIN 152..280
FT /note="Peptidase M15B"
FT /evidence="ECO:0000259|Pfam:PF02557"
FT REGION 21..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 303 AA; 34297 MW; B159F05F682C099A CRC64;
MKKTLRTIMM IMFVIPLSAC AIGDSGDEDP KNSTSSSERQ SQPDAKNKPD EDFEAKPESE
EQPPDNTEDE NQSSEDKDQD QLDNQKDSNS LNQEDSDSSN NSSNSAPKDV VEDHTSVEAI
INKQRQLPKG YIPSDLTVPD VPFYFEQFLP KKQMREEAAT HLEELFAAAS EQGLELVAAS
GYRSYERQKQ IYQSNVDAYG REEANKFSAQ PGHSEHQTGL AMDVTVAQVS FKLVQEFGKT
EEGDWLANHA HNYGFIIRYP KGKEDITGYS YEPWHLRYIG EETATEIYKN KQTLEEYFGL
VPE
//
