ID I0T9Z6_9BACT Unreviewed; 950 AA.
AC I0T9Z6;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Peptidase, S8/S53 family / Por secretion system C-terminal sorting domain multi-domain protein {ECO:0000313|EMBL:EID32449.1};
DE EC=3.4.21.- {ECO:0000313|EMBL:EID32449.1};
GN ORFNames=HMPREF9969_1417 {ECO:0000313|EMBL:EID32449.1};
OS Prevotella sp. oral taxon 306 str. F0472.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1095752 {ECO:0000313|EMBL:EID32449.1, ECO:0000313|Proteomes:UP000004421};
RN [1] {ECO:0000313|EMBL:EID32449.1, ECO:0000313|Proteomes:UP000004421}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0472 {ECO:0000313|EMBL:EID32449.1,
RC ECO:0000313|Proteomes:UP000004421};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240, ECO:0000256|RuleBase:RU003355}.
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:EID32449.1}.
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DR EMBL; AJIN01000067; EID32449.1; -; Genomic_DNA.
DR RefSeq; WP_009435820.1; NZ_AJIN01000067.1.
DR AlphaFoldDB; I0T9Z6; -.
DR STRING; 1095752.HMPREF9969_1417; -.
DR PATRIC; fig|1095752.3.peg.2136; -.
DR eggNOG; COG1404; Bacteria.
DR OrthoDB; 1489355at2; -.
DR Proteomes; UP000004421; Unassembled WGS sequence.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.1080; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR032304; Peptidase_S8_N.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR026444; Secre_tail.
DR NCBIfam; TIGR04183; Por_Secre_tail; 1.
DR PANTHER; PTHR42884:SF14; NEUROENDOCRINE CONVERTASE 1; 1.
DR PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF16361; Peptidase_S8_N; 1.
DR Pfam; PF18962; Por_Secre_tail; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..950
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003634963"
FT DOMAIN 77..183
FT /note="Subtilase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16361"
FT DOMAIN 212..535
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 874..946
FT /note="Secretion system C-terminal sorting"
FT /evidence="ECO:0000259|Pfam:PF18962"
FT ACT_SITE 219
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 268
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 495
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 950 AA; 104519 MW; 7AD71E4518ED2AA9 CRC64;
MKKFRNIYLS LISVALIAGL CTSCNDDMLE SSNQQTTTKP SNESFPWEPG MAYIKLKASV
SPTTRAATQT VSRAAILDDA TVKVEQVFDM TNEYANLKRA RGLDRWFVVK FDKAKDVGEV
INELKRDPAI EKVHGSVQIV PSEVTYTPTT RAPINPRRLR DANDGQGPLS FSDPYLKYQW
HYTTTIEQYM TFQPGADIDL FPAWQKETGD PHVVVAVMDS GIDFTHEDLE GAAWEGKDPK
TGETIHGRNF WAEETGQDNP NHIIAGAHGT HVAGTIAARN NNGIGVCGIA GGNGDANSGV
RLMSCEIYGH DGTTETATTK YIVKAFEFAA ENGASVMNCS WGYAFDRKKY LNNENFQSIF
KSQFDLLKDG IDYFTDVAGC DKDGKKKPDA YMKGGLIFFA SGNDSQYDID MIPASYNRVV
AVGAINSLGV PTAYMNKGPW VDVLAPGGTT ETGSVNQGVL STVPSDYEYG MTGPYPNTDF
TLPSDSHYAF AQGTSMATPH VTGIAALVVS KFGKTNPNFT NEDLRHRILG ALKDKNPYEV
KADENLAGKM GLGYIDALYA LSDPETEAPE APTITITDYS SHATKGYYDA NITWNVTADN
DALNDEHTAF AYDIQLFKKS DLSSPVQSFT RFSYNMSVGT EMQQEFTGLE TDMEYVVKIV
ARDRFNNRSQ EVSTNFKTRL NHAPIFTDMI EKNLRLLDTQ PYYHKILPVK DEDGHSWTYS
TTELPQGVEL KRIGDTFDLL IKVGAQGTYQ FDITLTDQLG GKTTQTIAYE VIPHTAPELT
SPIGDISLFA NGEAIEVNLA HAFTASSGKT MRYTVTSNNE QVAKVAVEGT KLIVTPGQKG
LTKLTITAID GSRRTTTSAI VRVTDKNAPD VHVIYPNPAH SYIKALMRSN VTKVRAIVTS
LHGQKLIDQS MTPDSRTHEV TLGIDRLAPG TYYLLLTTDR LTSKHVFIKK
//
