ID A0A1G2VVS5_9BACT Unreviewed; 301 AA.
AC A0A1G2VVS5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Peptidase S11 D-alanyl-D-alanine carboxypeptidase A N-terminal domain-containing protein {ECO:0000259|Pfam:PF00768};
GN ORFNames=A2542_01905 {ECO:0000313|EMBL:OHB25719.1};
OS Parcubacteria group bacterium RIFOXYD2_FULL_52_8.
OC Bacteria.
OX NCBI_TaxID=1817746 {ECO:0000313|EMBL:OHB25719.1, ECO:0000313|Proteomes:UP000177816};
RN [1] {ECO:0000313|EMBL:OHB25719.1, ECO:0000313|Proteomes:UP000177816}
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 -!- 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:OHB25719.1}.
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DR EMBL; MHXK01000007; OHB25719.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2VVS5; -.
DR Proteomes; UP000177816; Unassembled WGS sequence.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:InterPro.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0030655; P:beta-lactam antibiotic catabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:InterPro.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR000871; Beta-lactam_class-A.
DR InterPro; IPR001967; Peptidase_S11_N.
DR PANTHER; PTHR35333; BETA-LACTAMASE; 1.
DR PANTHER; PTHR35333:SF3; BETA-LACTAMASE2 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00768; Peptidase_S11; 2.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 4: Predicted;
FT DOMAIN 54..104
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT DOMAIN 117..271
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
SQ SEQUENCE 301 AA; 32045 MW; 0AAE266206149F8F CRC64;
MEQQRKKTRI LTLLSIGLLG LVAISVPQEP VAVTQAGAAP VQATRVLTLR TFVPPSLRAR
AAYVLDPTTG EVLFSRESDR PLPLASLTKV MTAIVAHESG KQQIRYSESE QEHAWATPQL
LSRMLVSSSN SAALAVASEV GKSFSEMTFI EAMNKKAVAL GLTKMQYRNP TGLDLPSGGS
GAEGTAEEVA QLLWYATKSA PELFSETSAA ELVTRALDGS RSRVLNTNEI VASLPSVRAS
KTGLTDLAGG NLAVVVDIAI DHPLVIVVLG SSESGRFTDT EKLVRAAKRY FVSDLAEADP
L
//
