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Database: UniProt
Entry: A0A1G6CZJ5_9FIRM
LinkDB: A0A1G6CZJ5_9FIRM
Original site: A0A1G6CZJ5_9FIRM 
ID   A0A1G6CZJ5_9FIRM        Unreviewed;       310 AA.
AC   A0A1G6CZJ5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=LD-carboxypeptidase LdcB, LAS superfamily {ECO:0000313|EMBL:SDB38258.1};
GN   ORFNames=SAMN02910317_01892 {ECO:0000313|EMBL:SDB38258.1};
OS   Ruminococcaceae bacterium FB2012.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae.
OX   NCBI_TaxID=1520817 {ECO:0000313|EMBL:SDB38258.1, ECO:0000313|Proteomes:UP000199364};
RN   [1] {ECO:0000313|EMBL:SDB38258.1, ECO:0000313|Proteomes:UP000199364}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FB2012 {ECO:0000313|EMBL:SDB38258.1,
RC   ECO:0000313|Proteomes:UP000199364};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FMXS01000009; SDB38258.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6CZJ5; -.
DR   STRING; 1520817.SAMN02910317_01892; -.
DR   OrthoDB; 9792074at2; -.
DR   Proteomes; UP000199364; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:SDB38258.1};
KW   Hydrolase {ECO:0000313|EMBL:SDB38258.1};
KW   Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:SDB38258.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199364};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        29..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          158..279
FT                   /note="Peptidase M15B"
FT                   /evidence="ECO:0000259|Pfam:PF02557"
FT   REGION          78..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   310 AA;  34633 MW;  F093D457FB3A596B CRC64;
     MSEKNKRKKK YVPRKGYTKE QYRRDTMQAY GVLTGIAMAL VIVLIYFMFI HKSADKQEKP
     VDVPQTVTVK KVISGETVSE VTADSDESKS VSETRPTSET QAAVTTTVTQ ATVETTVTAK
     KQEAEGHKLE VKNGITYVDG IMIVNKTYSL PADYAPGLDP TAEAAFNEMA SQAWSEGISL
     FICSGFRSYR EQDMLFRNYA ANRGQEEADR VSSRPGHSEH QSGLCMDVNT TEFDFAGTKE
     AIWLANNCAD YGFIIRFPLG KESVTGYAYE PWHIRYVGKK AAKEIFDKDI CLEEYLGVTS
     DYKNSTDQNG
//
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