ID E8V046_TERSS Unreviewed; 944 AA.
AC E8V046;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Peptidase S53 propeptide {ECO:0000313|EMBL:ADV82201.1};
GN OrderedLocusNames=AciPR4_1377 {ECO:0000313|EMBL:ADV82201.1};
OS Terriglobus saanensis (strain ATCC BAA-1853 / DSM 23119 / SP1PR4).
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Terriglobus.
OX NCBI_TaxID=401053 {ECO:0000313|EMBL:ADV82201.1, ECO:0000313|Proteomes:UP000006844};
RN [1] {ECO:0000313|EMBL:ADV82201.1, ECO:0000313|Proteomes:UP000006844}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC BAA-1853 / DSM 23119 / SP1PR4
RC {ECO:0000313|Proteomes:UP000006844};
RX PubMed=23450133; DOI=10.4056/sigs.3036810;
RA Rawat S.R., Mannisto M.K., Starovoytov V., Goodwin L., Nolan M., Hauser L.,
RA Land M., Davenport K.W., Woyke T., Haggblom M.M.;
RT "Complete genome sequence of Terriglobus saanensis type strain SP1PR4(T),
RT an Acidobacteria from tundra soil.";
RL Stand. Genomic Sci. 7:59-69(2012).
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; CP002467; ADV82201.1; -; Genomic_DNA.
DR RefSeq; WP_013567934.1; NC_014963.1.
DR AlphaFoldDB; E8V046; -.
DR STRING; 401053.AciPR4_1377; -.
DR KEGG; tsa:AciPR4_1377; -.
DR eggNOG; COG4934; Bacteria.
DR HOGENOM; CLU_004005_0_0_0; -.
DR OrthoDB; 127592at2; -.
DR Proteomes; UP000006844; Chromosome.
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; IPR000209; Peptidase_S8/S53_dom.
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; PF00082; Peptidase_S8; 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; PS51892; SUBTILASE; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000006844};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..944
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003232742"
FT TRANSMEM 880..898
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 227..640
FT /note="Peptidase S53"
FT /evidence="ECO:0000259|PROSITE:PS51695"
SQ SEQUENCE 944 AA; 95872 MW; 1128F21DC5E82A6C CRC64;
MRYGTTLRNV IPSLFCTFFL GFGSLSALAQ KPVARITAEI SNEQRTPIAG SRSPHALAAD
DAGAVPAGTK LEGMTLIFSR TTAQEADLQA LLAAQQDPTS PIYHQWLTVD QFAARFGVTD
ADIAKTTAWL QAQGFTVDRV SRSKDRIVFS GEAQQVASAF SPLRYYKSDG EKRYAPSADI
SIPTALSGIV KDVANLSNFR ARPHVRLNHS QAVASPNFTS SQTSSHYLTP GDITTIYDVK
AAYNAGYTGT GQSIAIMGQS AVVVSDIEKF QTAAGLPIKD PTLTLVPNTG SSTVYTGDES
ESDLDLEYSG GIAKGATIFF VYTGSSSNNG VFDSIAYAVD TQLATILSVS YGLCETELSA
SNFSSYNGVL EQAAAQGQTV IVSSGDDGST SCNDATTLTT AQRQALVVSF PASSQYVTAL
GGTEFTAAAV ATTNTTYWQA ASGSDVISSA LSYMPEMVWN DDSAANGLSS GGGGVSSMAP
RPTWQTGVTG IPSGNFRLVP DISLTSSASN AGYLYCSSDT TVGITGSCSN GFRDANSVYL
TVAGGTSFAA PVFAGMLAII NQKLNSTGQG NIDPTLYTLA SNAANYASAF HDITVGTNAC
TAGTCSTAGA SAYAATTGYD QATGLGSIDL YNLLTLWPTN AATATLAATT TTVSAASNTV
ASGVSDVITI TVASGSSTVT TVPAGTLTIT VDGTTTTKTL ALSTAGTATY TFSSTIAGAH
VIKAVYSGSA IYAASTGTAT VTVGAAGSGT GSFTLGATAV NLTAGNSGTS TVTVTPAGGY
TGTVAFNVTV SGSLSNACYT LNNAAITSTT AVTSALTIYT SSTACATVSS VSGSGMRKIT
STGVSRLESN SLPASPSNKA DIAVAGMLCL GLFGWRSRKL RLYVVLSLVT AIGFGISGCG
SSGSNSTTTA TTNATKGSYT LTITGTDSAT STITATTTTT LTIN
//
