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Database: UniProt
Entry: R6NFT1_9CLOT
LinkDB: R6NFT1_9CLOT
Original site: R6NFT1_9CLOT 
ID   R6NFT1_9CLOT            Unreviewed;       144 AA.
AC   R6NFT1;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Serine-type D-Ala-D-Ala carboxypeptidase {ECO:0000313|EMBL:CDC10993.1};
GN   ORFNames=BN649_01951 {ECO:0000313|EMBL:CDC10993.1};
OS   Clostridium sp. CAG:413.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1262803 {ECO:0000313|EMBL:CDC10993.1, ECO:0000313|Proteomes:UP000018076};
RN   [1] {ECO:0000313|EMBL:CDC10993.1, ECO:0000313|Proteomes:UP000018076}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:413 {ECO:0000313|Proteomes:UP000018076};
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:CDC10993.1}.
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DR   EMBL; CBES010000076; CDC10993.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6NFT1; -.
DR   STRING; 1262803.BN649_01951; -.
DR   Proteomes; UP000018076; Unassembled WGS sequence.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 2.60.410.10; D-Ala-D-Ala carboxypeptidase, C-terminal domain; 1.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR015956; Peniciliin-bd_prot_C_sf.
DR   InterPro; IPR012907; Peptidase_S11_C.
DR   InterPro; IPR037167; Peptidase_S11_C_sf.
DR   Pfam; PF07943; PBP5_C; 1.
DR   SMART; SM00936; PBP5_C; 1.
DR   SUPFAM; SSF69189; Penicillin-binding protein associated domain; 1.
PE   4: Predicted;
KW   Carboxypeptidase {ECO:0000313|EMBL:CDC10993.1};
KW   Hydrolase {ECO:0000313|EMBL:CDC10993.1};
KW   Protease {ECO:0000313|EMBL:CDC10993.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018076}.
FT   DOMAIN          35..125
FT                   /note="Peptidase S11 D-Ala-D-Ala carboxypeptidase A C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00936"
SQ   SEQUENCE   144 AA;  15372 MW;  4011F288378DE548 CRC64;
     MREGTHLVAV VMGSGNSSDR FETAKAMLNW GFSNFSTVTP KIDTTLIPDV GVINGVTERI
     TPRIPDADPI LIEKGRESEI AQKVDLALDV AAPVEQGQVL GTVTFSLGGE ELGKYSLTAP
     DSVPALTFGI IFRRILASLC GRVQ
//
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