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Database: UniProt
Entry: R6FTI1_9CLOT
LinkDB: R6FTI1_9CLOT
Original site: R6FTI1_9CLOT 
ID   R6FTI1_9CLOT            Unreviewed;       274 AA.
AC   R6FTI1;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase family protein {ECO:0000313|EMBL:CDB15385.1};
GN   ORFNames=BN542_00056 {ECO:0000313|EMBL:CDB15385.1};
OS   Clostridium sp. CAG:221.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1262780 {ECO:0000313|EMBL:CDB15385.1, ECO:0000313|Proteomes:UP000018176};
RN   [1] {ECO:0000313|EMBL:CDB15385.1, ECO:0000313|Proteomes:UP000018176}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:221 {ECO:0000313|Proteomes:UP000018176};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CDB15385.1}.
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DR   EMBL; CBDC010000061; CDB15385.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6FTI1; -.
DR   Proteomes; UP000018176; Unassembled WGS sequence.
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:CDB15385.1};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000313|EMBL:CDB15385.1};
KW   Protease {ECO:0000313|EMBL:CDB15385.1}.
FT   DOMAIN          118..244
FT                   /note="Peptidase M15B"
FT                   /evidence="ECO:0000259|Pfam:PF02557"
FT   COILED          52..79
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   274 AA;  31223 MW;  2AAD52DAD973A9F8 CRC64;
     MDFKKKKVDV AIFALLIVAL ISALLILGKD KIFTSAVDNN VHLEDESNVV SEEETADNSE
     ELEAEGNKVN EELENLLSIK NDPLMILVNK NNTLDSTYIP EDLVLSEIDF ISYIETRNLA
     KVTADAAKSM FEAAKKDGII LLGASGYRSY SVQENLYTSR VINDGQEEAD RYTAKPGQSE
     HQTGLALDIL SEDYQDMDDN FDSTEAYAWL KENCYKYGFI LRYPEGKEDI TGFLYEPWHY
     RYIGNNEVAK DIMDRNLTFE QYIEELDIKI QELS
//
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