ID A0A0A2EHQ3_PORCN Unreviewed; 933 AA.
AC A0A0A2EHQ3;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Por secretion system C-terminal sorting domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=HQ35_09500 {ECO:0000313|EMBL:KGN78458.1};
OS Porphyromonas cangingivalis.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=36874 {ECO:0000313|EMBL:KGN78458.1, ECO:0000313|Proteomes:UP000030125};
RN [1] {ECO:0000313|EMBL:KGN78458.1, ECO:0000313|Proteomes:UP000030125}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COT-109 OH1386 {ECO:0000313|Proteomes:UP000030125};
RA Wallis C., Deusch O., O'Flynn C., Davis I., Jospin G., Darling A.E.,
RA Coil D.A., Alexiev A., Horsfall A., Kirkwood N., Harris S., Eisen J.A.;
RT "Porphyromonas cangingivalis strain:COT-109_OH1386 Genome sequencing.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase C25 family.
CC {ECO:0000256|ARBA:ARBA00006067}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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:KGN78458.1}.
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DR EMBL; JQJD01000060; KGN78458.1; -; Genomic_DNA.
DR RefSeq; WP_036852743.1; NZ_JQJD01000060.1.
DR AlphaFoldDB; A0A0A2EHQ3; -.
DR STRING; 36874.HQ34_06845; -.
DR eggNOG; COG1404; Bacteria.
DR OrthoDB; 1489355at2; -.
DR Proteomes; UP000030125; Unassembled WGS sequence.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.10; 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; 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 PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF16361; Peptidase_S8_N; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 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}; Reference proteome {ECO:0000313|Proteomes:UP000030125};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT DOMAIN 53..202
FT /note="Subtilase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16361"
FT DOMAIN 227..519
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 234
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 290
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 487
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 933 AA; 102011 MW; 4AE197CC222AC567 CRC64;
MKNYVLLGTA ICAMSLFTNC KETYGFDDIE APSTDVSVRN HTNRYAPQNA VPGVLLVKVA
KTADVNLESF SASDLTLMGV SSPVMQAFKT LSVRSAERLF RPHPKFPNME KRFGLDRWYR
ITFDETKSLD MALQSFDGQR EFEVVEAEIR MQHPMSKSFS LPRPEPTEGI MVREAMIREE
ISKQTSFNDP ELHRQWHYHN TGNLSHGQLR ADINLFEAWK ITTGRPDVIV SIVDGELYVQ
HEDLVESLWR NPGEIPGDGI DNDKNNYIDD IYGYSFVNNT GTLLGDQLGH GTHVAGTIAA
RNNNGKGLCG IAGGDGTADS GVRIMSCAIF GKDELSGGNA DAIRYGANHG AVISQNSWGY
AYPATTMPVH VKDAIDYFIK VAGCDDQGNQ RPDSPMKGGV LFFAAGNDAL MFDAHPARYD
AVISVTAMAP SWKAASYTNY GLWTDIMAPG GELAHGDDHG VYSTMIPDCE WPQSKPGKLY
APMEGTSMAC PHVSGVAALV VSKFGGPGFT NEDLKQRILG GLRPVNITEK NLDYPISTLG
VGVIDAAMCL AENKGLAPED IKDLSADISY TEMTLSWSAV ADADDNFPVY YHLYSSAEPI
TSEADLAKAE LRKIPAYNIS PGTQLTANYS FLDDGRAYHY ALFAIDRWGL KSKIVYKTFT
TKKNTPPTGT FSTTLPVKVS KAMPVTFELK VKDAEGHAFE VGVHGESRGV SYSRKDDTVY
FTIRAVAPEG KHLALVDLTD ALGGRSTIEV PFEVIPYRAP ALETAFGNMV IGRDTETLSI
DLSDHFSLDP NFPIVCTVEV KDPSVATVKS EGGKLFITPG RNGVTRVTVY VTDGITEAVS
SSFDLSVVND KGDLVYSLSP NPVKTRLLLL VNPDMKKVDI DIRTIRGEQV YKKSMIVRAS
GKVPLNLKRL AMGTYTIYVK GELGVYKGSF VKL
//
