ID A0A1G0YEM9_9BACT Unreviewed; 363 AA.
AC A0A1G0YEM9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Peptidase S11 D-alanyl-D-alanine carboxypeptidase A N-terminal domain-containing protein {ECO:0000259|Pfam:PF00768};
GN ORFNames=A2X48_08640 {ECO:0000313|EMBL:OGV44351.1};
OS Lentisphaerae bacterium GWF2_49_21.
OC Bacteria; Lentisphaerota.
OX NCBI_TaxID=1798573 {ECO:0000313|EMBL:OGV44351.1, ECO:0000313|Proteomes:UP000178513};
RN [1] {ECO:0000313|EMBL:OGV44351.1, ECO:0000313|Proteomes:UP000178513}
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:OGV44351.1}.
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DR EMBL; MHBH01000001; OGV44351.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G0YEM9; -.
DR STRING; 1798573.A2X48_08640; -.
DR Proteomes; UP000178513; 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:SF34; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACC; 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 81..311
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT REGION 337..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 111
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 114
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 172
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 283
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 363 AA; 40030 MW; 68B9E014CCD02175 CRC64;
MKKLLITFSI VAVVIVAHVI LLRHFIFPEK KTPPVEETKP ADPIDNSKIP PPQDIPVVKH
KYSPFNYRGA VIGDLPTVPT SKDATSGILV DLGSRKVLWA KNPRKAVAIA SMTKMMTELI
IFEDLENRKD VTLETQIQVT KSAYKIGGSQ IWLDPRESFS LEDLLKAVMI KSANDAAYLV
AEYFGNGDVY AFVEKMNTRS MELKLPGAKF YNPHGLPGDT AAEDNTCSPE GCAMLAERLL
DIPKAAEFAR TKLDYIRVGT PKQTALANHN HLIGACAGVN GMKTGWIQRS GFCITATCER
AGRKMVAVVT GFPSYKTRDA FVAKLLDWGY RQKPVEDKAP AEATQPGNEE KNLEDLLNQV
VPK
//
