ID D5EUG9_PRER2 Unreviewed; 409 AA.
AC D5EUG9;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase/D-alanyl-D-alanine-endopeptidase {ECO:0000313|EMBL:ADE82718.1};
DE EC=3.4.16.4 {ECO:0000313|EMBL:ADE82718.1};
GN Name=dacB {ECO:0000313|EMBL:ADE82718.1};
GN OrderedLocusNames=PRU_1998 {ECO:0000313|EMBL:ADE82718.1};
OS Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Xylanibacter.
OX NCBI_TaxID=264731 {ECO:0000313|EMBL:ADE82718.1, ECO:0000313|Proteomes:UP000000927};
RN [1] {ECO:0000313|EMBL:ADE82718.1, ECO:0000313|Proteomes:UP000000927}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19189 / JCM 8958 / 23 {ECO:0000313|Proteomes:UP000000927};
RX PubMed=20585943; DOI=10.1007/s00248-010-9692-8;
RG North American Consortium for Rumen Bacteria;
RA Purushe J., Fouts D.E., Morrison M., White B.A., Mackie R.I.,
RA Coutinho P.M., Henrissat B., Nelson K.E.;
RT "Comparative genome analysis of Prevotella ruminicola and Prevotella
RT bryantii: insights into their environmental niche.";
RL Microb. Ecol. 60:721-729(2010).
CC -!- SIMILARITY: Belongs to the peptidase S13 family.
CC {ECO:0000256|ARBA:ARBA00006096}.
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DR EMBL; CP002006; ADE82718.1; -; Genomic_DNA.
DR RefSeq; WP_013064704.1; NC_014033.1.
DR AlphaFoldDB; D5EUG9; -.
DR STRING; 264731.PRU_1998; -.
DR KEGG; pru:PRU_1998; -.
DR eggNOG; COG2027; Bacteria.
DR HOGENOM; CLU_017692_1_3_10; -.
DR Proteomes; UP000000927; Chromosome.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
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; 2.
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:ADE82718.1};
KW Hydrolase {ECO:0000313|EMBL:ADE82718.1};
KW Protease {ECO:0000313|EMBL:ADE82718.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000927};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..409
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003071836"
SQ SEQUENCE 409 AA; 44947 MW; D4E22E2496C038EB CRC64;
MKQNIRNWIF SLLLAGTVGS LQAQTVDTLV VDTCATDTIV ELPWPQNLQA RLDTLTSDRM
FDYTQLGLMV YDITADSTLY TYGAKQILRP ASTMKLLTAI TALDQLGIKH KFRTSLYYTG
EVVDSVLVGD LYCEGGMDPL FDTTDMKAFS ASVKALGIHT VKGKLVDVNT FKDQDLLGEG
WCWDDDNPSL SSLLINGKDD FISQFAQQLD KDSIFPDGPA EYAALPKDAV LLCQRSHSLE
DVLVPMMKDS NNLYAESVFY QIGAATGARP AKSSHARNAI KRTLHKAGIT GSHYKIADGS
GLSLYNYVTP ELLTKLLVYA YRHPSIYRYL YVSLPVAGED GTLKKRMKDT PAQISVRAKT
GTLTGISSLA GYAVATNNHV LAFAIINQGV MKNDQGRNFQ DKVCTAMCK
//
