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
//