ID A0A1G2I4R2_9BACT Unreviewed; 312 AA.
AC A0A1G2I4R2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Peptidase S11 D-alanyl-D-alanine carboxypeptidase A N-terminal domain-containing protein {ECO:0000259|Pfam:PF00768};
GN ORFNames=A3F47_02485 {ECO:0000313|EMBL:OGZ69617.1};
OS Candidatus Staskawiczbacteria bacterium RIFCSPHIGHO2_12_FULL_38_11.
OC Bacteria; Candidatus Staskawiczbacteria.
OX NCBI_TaxID=1802209 {ECO:0000313|EMBL:OGZ69617.1, ECO:0000313|Proteomes:UP000179214};
RN [1] {ECO:0000313|EMBL:OGZ69617.1, ECO:0000313|Proteomes:UP000179214}
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:OGZ69617.1}.
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DR EMBL; MHOV01000031; OGZ69617.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2I4R2; -.
DR Proteomes; UP000179214; Unassembled WGS sequence.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; 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 Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR018044; Peptidase_S11.
DR InterPro; IPR001967; Peptidase_S11_N.
DR PANTHER; PTHR21581; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR21581:SF6; TRAFFICKING PROTEIN PARTICLE COMPLEX SUBUNIT 12; 1.
DR Pfam; PF00768; Peptidase_S11; 1.
DR PRINTS; PR00725; DADACBPTASE1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 68..276
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 104
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 107
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 159
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 263
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 312 AA; 34718 MW; C7FA17E85A353347 CRC64;
MAIVKILKHS LLLFVFVFLS ACSFYAIDFL IAGAGGFFST KAAASVSDGF ESEIVKIENT
ENPIIKQKEE FSINAESFIS IKAENGQYNI LLSKNEQDKL PVASLTKLMT ALVVLDNYDL
NQKVTVSKLA MAQEGEQGNL KEGEVLSVKN LLYISLIESS NRASFALSEV VGADEFIILM
NNKAQDMGLQ NTYFADSSGL LENSTSSSED LAKLSIYLFE NYPLFREIIN FKEFDLYING
RLHHKLVNTN KFLGEVPGVV GGKTGWTIFS KGCFMVVQEI PGTGNYLLHI ILGADDRFLE
MQKLIDWVRA HY
//
