ID R5GSX3_9BACT Unreviewed; 416 AA.
AC R5GSX3;
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/D-alanyl-D-alanine-endopeptidase {ECO:0000313|EMBL:CCY15867.1};
GN ORFNames=BN773_01807 {ECO:0000313|EMBL:CCY15867.1};
OS Prevotella sp. CAG:755.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1262935 {ECO:0000313|EMBL:CCY15867.1, ECO:0000313|Proteomes:UP000018353};
RN [1] {ECO:0000313|EMBL:CCY15867.1, ECO:0000313|Proteomes:UP000018353}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:755 {ECO:0000313|Proteomes:UP000018353};
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 -!- SIMILARITY: Belongs to the peptidase S13 family.
CC {ECO:0000256|ARBA:ARBA00006096}.
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:CCY15867.1}.
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DR EMBL; CAXR010000107; CCY15867.1; -; Genomic_DNA.
DR AlphaFoldDB; R5GSX3; -.
DR STRING; 1262935.BN773_01807; -.
DR Proteomes; UP000018353; Unassembled WGS sequence.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.50.80.20; D-Ala-D-Ala carboxypeptidase C, peptidase S13; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR000667; Peptidase_S13.
DR NCBIfam; TIGR00666; PBP4; 1.
DR PANTHER; PTHR30023; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR30023:SF0; PENICILLIN-SENSITIVE CARBOXYPEPTIDASE A; 1.
DR Pfam; PF02113; Peptidase_S13; 2.
DR PRINTS; PR00922; DADACBPTASE3.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:CCY15867.1};
KW Hydrolase {ECO:0000313|EMBL:CCY15867.1};
KW Protease {ECO:0000313|EMBL:CCY15867.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018353}.
SQ SEQUENCE 416 AA; 45206 MW; 0D94A3E69AB27CD6 CRC64;
MKREFVHIII YIAAISVWLA GWQADAQTFT IRSVIAEREA QAAADSSLDW PDHLQARLSE
LVCNPMFEHS QLGLYVYDLT ADSALFEQGK RQLLRPASTQ KLLTAITALA QLGGSYRFET
SIYRTGELAD SVLHGDLYVV GGFDPRFGYD DLRAMVDKLA SSGVRRIDGR LFLDVSMKDT
LAWGWGWCWD DELAPLSPLT VNGHDDFSAA LFRALGSVGI SFVGAIENAV RPAGAVLVAS
RHHSMDQILT EALKESNNHY AEALFYQLGA QDGMAYPSGE ESARCVERLV TSLGLPFSDC
RVADGSGLSL YNYLTPEVLV AALRYAYQNS EIYAHLKPAL PVAGCDGTLR RRMTTGNACA
NVFAKTGTVE GVSTLAGYAA AANGHLLCFA IMNQGVLSQA PARRFQDSVC EALTSP
//