ID A0A1G0Y623_9BACT Unreviewed; 335 AA.
AC A0A1G0Y623;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Peptidase S49 domain-containing protein {ECO:0000259|Pfam:PF01343};
GN ORFNames=A2X46_16145 {ECO:0000313|EMBL:OGV41360.1};
OS Lentisphaerae bacterium GWF2_57_35.
OC Bacteria; Lentisphaerota.
OX NCBI_TaxID=1798576 {ECO:0000313|EMBL:OGV41360.1, ECO:0000313|Proteomes:UP000178598};
RN [1] {ECO:0000313|EMBL:OGV41360.1, ECO:0000313|Proteomes:UP000178598}
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 S49 family.
CC {ECO:0000256|ARBA:ARBA00008683}.
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:OGV41360.1}.
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DR EMBL; MHBK01000065; OGV41360.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G0Y623; -.
DR STRING; 1798576.A2X46_16145; -.
DR Proteomes; UP000178598; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd07023; S49_Sppa_N_C; 1.
DR InterPro; IPR001907; ClpP.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR004635; Pept_S49_SppA.
DR InterPro; IPR002142; Peptidase_S49.
DR InterPro; IPR047272; S49_SppA_C.
DR NCBIfam; TIGR00706; SppA_dom; 1.
DR PANTHER; PTHR42987; PEPTIDASE S49; 1.
DR PANTHER; PTHR42987:SF4; PROTEASE SLR0021-RELATED; 1.
DR Pfam; PF01343; Peptidase_S49; 1.
DR PRINTS; PR00127; CLPPROTEASEP.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022670};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 141..286
FT /note="Peptidase S49"
FT /evidence="ECO:0000259|Pfam:PF01343"
SQ SEQUENCE 335 AA; 37128 MW; 2A2DF6C7EA6F2DFE CRC64;
MNNGRKCSHA GFWVALVFLG GGLLLSLAMN AGLMAALLGK KTSAGFTGNA EDEYPQMTEK
WSYGEGKVKA ARIGFTGVIT RNVERDIFGF SFDQVESVLR QIRAAKNDSD VKAIVFEVDS
PGGEITPSDE IYQALLEFKA SDENRKVIVF VTGMAASGGY YMSAAGDWIL AEPTSIIGSI
GVIMESINFK GLSEKIGITD VTIKSSENKD LLNPFREVSP VHVAILQATV DAFYQRFFNI
VQNSRPIDED KLIDMADGRI FSAEVALETR FIDEIGYWDD VVSRTHAVLE EDQVKFIRYE
QATSFFDRLS QARAPLSPMS LLKPATPRFL YQWRP
//
