ID A0A1J5H6K5_9BACT Unreviewed; 353 AA.
AC A0A1J5H6K5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Peptidase S11 D-alanyl-D-alanine carboxypeptidase A N-terminal domain-containing protein {ECO:0000259|Pfam:PF00768};
GN ORFNames=AUK20_00960 {ECO:0000313|EMBL:OIP80861.1};
OS Parcubacteria group bacterium CG2_30_45_37.
OC Bacteria.
OX NCBI_TaxID=1805319 {ECO:0000313|EMBL:OIP80861.1, ECO:0000313|Proteomes:UP000183231};
RN [1] {ECO:0000313|EMBL:OIP80861.1, ECO:0000313|Proteomes:UP000183231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG2_30_45_37 {ECO:0000313|EMBL:OIP80861.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(2016).
CC -!- SIMILARITY: Belongs to the peptidase S11 family.
CC {ECO:0000256|ARBA:ARBA00007164, ECO:0000256|RuleBase:RU004016}.
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:OIP80861.1}.
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DR EMBL; MNZH01000022; OIP80861.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J5H6K5; -.
DR Proteomes; UP000183231; 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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
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; IPR018044; Peptidase_S11.
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; 1.
DR PRINTS; PR00725; DADACBPTASE1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 102..332
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 137
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 140
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 192
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 301
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 353 AA; 38064 MW; BABD76A1EA6BB9C8 CRC64;
MLIPAAISLI LSAVFLNLSL LFPGTVSFPG GFEPVKVGRV MGVSASAAGD VLIEQNENFN
KAIVRVVADA KALPLPALPQ LPSLDLPLVR LPENQEKAAE ADKTGYDLPA ENGVILDCQN
NSLYFAKRSD RQWPIASITK LFTAYTFLDD NPGWETSLTI EARDKRDGGK IYLFAGDIVK
VKDLFYFSLV GSDNTATAAL VRSTGLSEAE FVQKMNLKIK ELGLVNTRLV DAVGLKDGNI
STAREVAEFA CLALARPEIS RASLTKKYEF TTQPGRIKSI TSTNELLASF PQGGVNILGG
KTGFINLAGY CFVGQFANQA GEVIVTVILG ADSDSGRFAL TKKLVELYYG RQQ
//
