ID A0A1G1YSP1_9BACT Unreviewed; 444 AA.
AC A0A1G1YSP1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Peptidase S11 D-alanyl-D-alanine carboxypeptidase A N-terminal domain-containing protein {ECO:0000259|Pfam:PF00768};
GN ORFNames=A2912_02515 {ECO:0000313|EMBL:OGY55289.1};
OS Candidatus Buchananbacteria bacterium RIFCSPLOWO2_01_FULL_40_23b.
OC Bacteria; Candidatus Buchananbacteria.
OX NCBI_TaxID=1797544 {ECO:0000313|EMBL:OGY55289.1, ECO:0000313|Proteomes:UP000178122};
RN [1] {ECO:0000313|EMBL:OGY55289.1, ECO:0000313|Proteomes:UP000178122}
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 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:OGY55289.1}.
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DR EMBL; MHIN01000018; OGY55289.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1YSP1; -.
DR Proteomes; UP000178122; 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 221..428
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 231
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 234
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 295
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 403
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 444 AA; 50382 MW; DA566EBB922C9618 CRC64;
MAEWHQLFRC STEGGTPHRP PQADWCAGKL FSKMKGMPTL IKIKIIIPAL ILFLFLPLKP
IQAADLSVAK KYAGRFLLQT ESYGRAWYVE PKTFERYYFK DAKTALEVTE LLGLGITNVD
LEKIPTEKGQ KFDRRLVNRL KGRLLIAVEK NGEAWYVNPV DNLRYYLKDE TIFDLIKKFH
IAVKNKELSQ VPMNQKQIVC DYTFADVAYV RYDGKNFTKS YNSEVILPLA SLTKLMTALV
LLDLNPDWQK KITITAAQLN YPKNYVADDA TSEVDFQLGD TLSFYDLWVA MLVSSANQAT
AALVDSSGID RADFVEKMNQ KAKDLGLKKT IFYDLAGLDA HNVTTTKEMA KLALAAFAKP
EISETTTIRD YNLSALDKTG TAKSIKTTNR NFSLFQYEPQ AVKTGYLVEA QRTMVLKKNN
AIIVVMHALS MKQRNQTIEY LLKQ
//
