ID B1C4W5_9FIRM Unreviewed; 342 AA.
AC B1C4W5;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE SubName: Full=Serine-type D-Ala-D-Ala carboxypeptidase {ECO:0000313|EMBL:EDS73709.1};
GN ORFNames=CLOSPI_02134 {ECO:0000313|EMBL:EDS73709.1};
OS Thomasclavelia spiroformis DSM 1552.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Coprobacillaceae; Thomasclavelia.
OX NCBI_TaxID=428126 {ECO:0000313|EMBL:EDS73709.1, ECO:0000313|Proteomes:UP000004910};
RN [1] {ECO:0000313|EMBL:EDS73709.1, ECO:0000313|Proteomes:UP000004910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1552 {ECO:0000313|EMBL:EDS73709.1,
RC ECO:0000313|Proteomes:UP000004910};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Clostridium spiroforme (DSM 1552).";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDS73709.1, ECO:0000313|Proteomes:UP000004910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1552 {ECO:0000313|EMBL:EDS73709.1,
RC ECO:0000313|Proteomes:UP000004910};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2008) 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:EDS73709.1}.
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DR EMBL; ABIK02000015; EDS73709.1; -; Genomic_DNA.
DR AlphaFoldDB; B1C4W5; -.
DR STRING; 428126.CLOSPI_02134; -.
DR eggNOG; COG1876; Bacteria.
DR HOGENOM; CLU_058389_0_0_9; -.
DR OrthoDB; 9792074at2; -.
DR Proteomes; UP000004910; 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:EDS73709.1};
KW Hydrolase {ECO:0000313|EMBL:EDS73709.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:EDS73709.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000004910};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 183..312
FT /note="Peptidase M15B"
FT /evidence="ECO:0000259|Pfam:PF02557"
SQ SEQUENCE 342 AA; 40838 MW; FE78D15F164648FB CRC64;
MLMLHRKRRV SRENIIVIIG ILVILMGFVF FNFERINLFL KGYSFSEQSV ILNLDDETVK
RFLNNSELID IKSWNDIDND KHYLEYQKYQ EYKKQLSKKE VIGYIDTFYD KYYKKLIKLN
YTYDQMISLM KHALINDFQI LIDNNYSYSK IQPYLNINGI TFKDISKYIS SNKEPIAPDC
NNKKLRKDAA KALEEMYQDA LKKGYHLVLN SGYRSYESQM EIYEEYFRKY DKITASKLVS
KPGSSEHQLG LGVNLTSQSV VDKKRMVFGD SDEYKWVVKN AHKYGFILRY PKDRSSFTGI
VNEPWHFRYV GKKIAKIIYD NDWILEDYIL KYGFDYELKM IR
//