ID A0A1F7VFV8_9BACT Unreviewed; 297 AA.
AC A0A1F7VFV8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-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=A3H75_03165 {ECO:0000313|EMBL:OGL89412.1};
OS Candidatus Uhrbacteria bacterium RIFCSPLOWO2_02_FULL_51_9.
OC Bacteria; Candidatus Uhrbacteria.
OX NCBI_TaxID=1802410 {ECO:0000313|EMBL:OGL89412.1, ECO:0000313|Proteomes:UP000176678};
RN [1] {ECO:0000313|EMBL:OGL89412.1, ECO:0000313|Proteomes:UP000176678}
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:OGL89412.1}.
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DR EMBL; MGES01000004; OGL89412.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F7VFV8; -.
DR STRING; 1802410.A3H75_03165; -.
DR Proteomes; UP000176678; 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.
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, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..297
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009533257"
FT DOMAIN 36..267
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 65
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 68
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 121
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 240
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 297 AA; 32879 MW; 27A97B420D84F3A1 CRC64;
MSKYLTFLIF SATLAFPLAS PVFAAEKLPP NNAGFQSRAA SVLILNDNSS ELAGKASDVV
RPIASLTKLM TAIVLLDNGL DFSKTATYTP EKHYAYKNYM NIKRGEVFRV SDLWFGMLTG
SLNVETRMLV DAVGIPETTF VNKMNIKASV LGLEYTKFFN VTGLSADLVR GQKAENVSTA
RELAALFQEA LKYPQIAGAL SLPAYRFEEV VDKDKKTGHY FHHTNKLMQE ALPYRIVASK
TGYTEEAGAC FVTLTTSRAG NHLIVSLGDP NYQRRFDEPK RLAEWALLET RVRAAGQ
//
