ID A0A011RMK8_9LACT Unreviewed; 361 AA.
AC A0A011RMK8;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:EXJ23118.1};
DE EC=3.4.16.4 {ECO:0000313|EMBL:EXJ23118.1};
GN ORFNames=ADIAL_1403 {ECO:0000313|EMBL:EXJ23118.1};
OS Alkalibacterium sp. AK22.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Alkalibacterium.
OX NCBI_TaxID=1229520 {ECO:0000313|EMBL:EXJ23118.1, ECO:0000313|Proteomes:UP000020164};
RN [1] {ECO:0000313|EMBL:EXJ23118.1, ECO:0000313|Proteomes:UP000020164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK22 {ECO:0000313|Proteomes:UP000020164};
RA Singh A., Pinnaka A.K.;
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
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:EXJ23118.1}.
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DR EMBL; JANL01000033; EXJ23118.1; -; Genomic_DNA.
DR RefSeq; WP_051503791.1; NZ_JANL01000033.1.
DR AlphaFoldDB; A0A011RMK8; -.
DR STRING; 1229520.ADIAL_1403; -.
DR MEROPS; M15.024; -.
DR PATRIC; fig|1229520.3.peg.1368; -.
DR eggNOG; COG1876; Bacteria.
DR eggNOG; COG3807; Bacteria.
DR OrthoDB; 9792074at2; -.
DR Proteomes; UP000020164; Unassembled WGS sequence.
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 Gene3D; 2.30.30.40; SH3 Domains; 2.
DR InterPro; IPR009045; Hedgehog_sig/DD-Pept_Zn-bd_sf.
DR InterPro; IPR003709; Pept_M15B.
DR InterPro; IPR003646; SH3-like_bac-type.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR PANTHER; PTHR34385; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR34385:SF1; PEPTIDOGLYCAN L-ALANYL-D-GLUTAMATE ENDOPEPTIDASE CWLK; 1.
DR Pfam; PF08239; SH3_3; 2.
DR Pfam; PF02557; VanY; 1.
DR SMART; SM00287; SH3b; 2.
DR SUPFAM; SSF55166; Hedgehog/DD-peptidase; 1.
DR SUPFAM; SSF50044; SH3-domain; 2.
DR PROSITE; PS51781; SH3B; 2.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000313|EMBL:EXJ23118.1};
KW Hydrolase {ECO:0000313|EMBL:EXJ23118.1};
KW Protease {ECO:0000313|EMBL:EXJ23118.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000020164}.
FT DOMAIN 40..102
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
FT DOMAIN 120..182
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
SQ SEQUENCE 361 AA; 40283 MW; 8A81D22D37944B21 CRC64;
MNTAQLKRSF LLLTIFLSGL LLANMTLNET DPFDQFVSAS TLEYQTTANL NLRSGASTRH
KILLTIPRGQ KVEYLSKSGS WYRVRYNGRT GFVSSSYLRK VPAVAPAKQT TAKPAAAPKS
QTSYETTANL NLRSGASTRH KILLTIPRGQ KVDFISRSGS WFQVRYKGTT GFVSSAYLKA
APASKAAAPK AEIKPTYVNG VLLVNKHYGL PAHFAPGENK EARAAFNRMA QAAAKDGIRL
TAFSTYRSFE RQRTLYNNYV KKDGQKAADR YSARPGHSEH QTGLAFDVSQ TGAKNPFAES
HATRWMARHA HTYGFIVRYP KGKEHITGYM YEPWHLRYLG PDLAGKVYRS HLTLEEYLGI
K
//