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Database: UniProt
Entry: A0A011RMK8_9LACT
LinkDB: A0A011RMK8_9LACT
Original site: A0A011RMK8_9LACT 
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
//
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