ID A0A1G3QEQ0_9SPIR Unreviewed; 499 AA.
AC A0A1G3QEQ0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase/D-alanyl-D-alanine-endopeptidase {ECO:0000313|EMBL:OHD64759.1};
GN ORFNames=A2176_10545 {ECO:0000313|EMBL:OHD64759.1};
OS Spirochaetes bacterium RBG_13_51_14.
OC Bacteria; Spirochaetota.
OX NCBI_TaxID=1802193 {ECO:0000313|EMBL:OHD64759.1, ECO:0000313|Proteomes:UP000176595};
RN [1] {ECO:0000313|EMBL:OHD64759.1, ECO:0000313|Proteomes:UP000176595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OHD64759.1}.
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DR EMBL; MIBH01000041; OHD64759.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G3QEQ0; -.
DR STRING; 1802193.A2176_10545; -.
DR Proteomes; UP000176595; 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; 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; 1.
DR PRINTS; PR00922; DADACBPTASE3.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:OHD64759.1};
KW Hydrolase {ECO:0000313|EMBL:OHD64759.1};
KW Protease {ECO:0000313|EMBL:OHD64759.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..499
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009598478"
SQ SEQUENCE 499 AA; 55165 MW; 0A5760C36D9B823D CRC64;
MPLQFFFKSI AMAAAPILIA AGCGFRPVDV DVSFGPGKPA DGAEMDLIKN MPPDNIGFIL
YDLERKSVVK IHNRSRAFIP ASTTKVFTTV AAMNVLGPDY RFGTRISYRG SISGGTLKGD
LYLKGTGDPL LTVADLMDMS DAMKKKGIAS VSGRFYYDES DLASTVSIDG DMEPDVSFNP
GVSALSLDYN SISAEWKRDR ERGAMDIFLT PSLPINHAGL SAEKLRENIT FAYQNRSGTE
SWFLSPDKDT DGIERLPVKK PALYTAYMFS TICGMRGIRL PRPEPGTEPG CARTIAYHES
SELTDIADLT LTFSINLAAE LMMLTTAKKI TGEKMNLADS AKTISAYFSD RLESVSWRYF
RIINGSGLTA KNRITPEQMV AVLAYADAQN YSGRKYRSCL PASGWEWSLM NRLNDPETAF
HVWAKTGSIN YALALAGYLY TKSSRSMAFA IFVNDIAKRE RYDADPDRRS SASARRVNTW
LKNSKTVMDH IVTGWITEL
//
