ID A0A1Q7T3K7_9BACT Unreviewed; 946 AA.
AC A0A1Q7T3K7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Peptidase S53 {ECO:0000313|EMBL:OLD83097.1};
GN ORFNames=AUF67_01955 {ECO:0000313|EMBL:OLD83097.1};
OS Acidobacteria bacterium 13_1_20CM_58_21.
OC Bacteria; Acidobacteriota.
OX NCBI_TaxID=1803438 {ECO:0000313|EMBL:OLD83097.1, ECO:0000313|Proteomes:UP000186215};
RN [1] {ECO:0000313|EMBL:OLD83097.1, ECO:0000313|Proteomes:UP000186215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
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:OLD83097.1}.
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DR EMBL; MNIJ01000024; OLD83097.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7T3K7; -.
DR Proteomes; UP000186215; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd04056; Peptidases_S53; 1.
DR CDD; cd11377; Pro-peptidase_S53; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR032109; Big_3_5.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015366; S53_propep.
DR InterPro; IPR030400; Sedolisin_dom.
DR PANTHER; PTHR14218:SF42; PEPTIDASE S53 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR14218; PROTEASE S8 TRIPEPTIDYL PEPTIDASE I CLN2; 1.
DR Pfam; PF16640; Big_3_5; 1.
DR Pfam; PF09286; Pro-kuma_activ; 1.
DR SMART; SM00944; Pro-kuma_activ; 1.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51695; SEDOLISIN; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 851..875
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 882..905
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 230..646
FT /note="Peptidase S53"
FT /evidence="ECO:0000259|PROSITE:PS51695"
SQ SEQUENCE 946 AA; 97094 MW; 8A9BC8EF3E489B63 CRC64;
MQTLLRTCVR RGVHFGIWFT VLTSLAISLP AQERAERVTA EIDDTERTAI QGSQPPMARP
ENDAGRMAVG TKLEGISIVL SRTVTQEAAL QALIAAQQDP TSPSYHKWLT PEEFAARFGV
ADTDIAKIQS WLEKHGFTVD SISRSKNRII FSGTVEQVES AFGTELHYYK VNGEAHFAPS
RDISMPVAVS SVVQTVTNLS TFRPKPHVRF MSPQPAVSPN FSSGQSGNHF LTPKDVATIY
DINPAYHAGY TGTGQAIAVV GQSSILLSDI EHFQTAAGFT PLKDPTLVLV PGSGTAMVRT
GDEGESDLDL EYSSTIANGA TIYFVYVGNN ANYNVFDAIQ YAVDNKIAPV ISVSYGLCEA
GLGQTGYSSL NLFLAQAATQ GQSVIAASGD SGSTDCYGVM GLTTAQQEAL AVDFPASSQY
VTGMGGSEFL APDVAASNTT YWQAGSGSDV VSSALSYIPE QVWNDDSSQA GLSSGGGGVS
VLTARPSWQT GVTGIPSGNF RLMPDISLSS SPNNAGYLYC SSDSTTRVTG SCANGFRDSN
NTNLTVAGGT SFAAPIFAGM LAIINGKLNS TGQGVVNRTL YALAANSTTY AAAFHDITSG
GNQCTAGTTY CSTAGTSEYP ATTGFDEASG LGSIDFFNLL TVWPGSSTVL VPSKTTLSAA
TATPAAGAND AITITVASGS SSSTATPTGT LTIAVDGTTQ TSSLALVNGA AVYTFSSMTT
DSHTITATYS GDSVYASSSS SLTVTVAANK AFKLAATSVT VSAGNAGTST VTVTPQSGYT
GTVAWTISSS PSLLNGCFVL PNTTVAGTSA VAATLTLYTI ASSCTNSAVV LASSRRDILL
GGVPIASRDE LLLFSPLHAT QASMAIAGLL IVGLLGRRSR RLATLAGICT LAVVGLAASG
CAGGLSGAPS SSTPRAAKGT YTITIVGADT ASPSITAAIT MTLTIN
//