ID J6H3L2_9PORP Unreviewed; 610 AA.
AC J6H3L2;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Signal peptide peptidase SppA, 67K type {ECO:0000313|EMBL:EJU17658.1};
DE EC=3.4.-.- {ECO:0000313|EMBL:EJU17658.1};
GN Name=sppA {ECO:0000313|EMBL:EJU17658.1};
GN ORFNames=HMPREF1323_0635 {ECO:0000313|EMBL:EJU17658.1};
OS Porphyromonas sp. oral taxon 279 str. F0450.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=1125723 {ECO:0000313|EMBL:EJU17658.1, ECO:0000313|Proteomes:UP000004156};
RN [1] {ECO:0000313|EMBL:EJU17658.1, ECO:0000313|Proteomes:UP000004156}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0450 {ECO:0000313|EMBL:EJU17658.1,
RC ECO:0000313|Proteomes:UP000004156};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
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:EJU17658.1}.
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DR EMBL; ALKJ01000013; EJU17658.1; -; Genomic_DNA.
DR RefSeq; WP_009432440.1; NZ_ALKJ01000013.1.
DR AlphaFoldDB; J6H3L2; -.
DR PATRIC; fig|1125723.3.peg.384; -.
DR Proteomes; UP000004156; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
DR CDD; cd07018; S49_SppA_67K_type; 1.
DR CDD; cd07023; S49_Sppa_N_C; 1.
DR Gene3D; 6.20.330.10; -; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR004634; Pept_S49_pIV.
DR InterPro; IPR004635; Pept_S49_SppA.
DR InterPro; IPR002142; Peptidase_S49.
DR InterPro; IPR047217; S49_SppA_67K_type_N.
DR InterPro; IPR047272; S49_SppA_C.
DR NCBIfam; TIGR00705; SppA_67K; 1.
DR NCBIfam; TIGR00706; SppA_dom; 1.
DR PANTHER; PTHR33209; PROTEASE 4; 1.
DR PANTHER; PTHR33209:SF1; SERINE PROTEASE SPPA, CHLOROPLASTIC; 1.
DR Pfam; PF01343; Peptidase_S49; 2.
DR PIRSF; PIRSF001217; Protease_4_SppA; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EJU17658.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000004156};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..48
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 137..291
FT /note="Peptidase S49"
FT /evidence="ECO:0000259|Pfam:PF01343"
FT DOMAIN 387..542
FT /note="Peptidase S49"
FT /evidence="ECO:0000259|Pfam:PF01343"
FT ACT_SITE 205
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001217-1"
FT ACT_SITE 402
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001217-1"
SQ SEQUENCE 610 AA; 66508 MW; 619D91F4D2CF053E CRC64;
MEEPLQPKKP LGFWKTVLAS FVGFIAANIL CSIFAFFLFI VIVVGALASG STPTEIRDGS
VLKIDLSSIS EIVTTDELSS FIPGMASDEK PISLSQALAS IRKAKSDSRI RGIYLNVEGY
SGGMASTADL REALKDFRSS GKFIISYADS YDQKAYYLSS VANQVILNPQ GMVGLVGLAS
APTFYRQALD KLGVKAHIFK VGTYKGAVEP FMLDKLSEPN REQISVYLNG LWDFMLREIS
ASRSVPVDSL RAFADSGRAF GEAETFVRAH LVDTLAYRLD VEDLMAQRLD VASADDIPVV
TLSDFLMEPD PLDKGRTDKD NAVKVLFAEG EITESPLSSD GITSDLARDL RALRDDPTAK
AVVLRINSPG GSAFLSEQIW HEVRELSQSR TVVVSMGDVA ASGGYYIASA ADAIVASPVT
LTGSIGIFGI LPDASELGRK VGVSIDVVQT SPYADMSMSD PMAMLLRPLT PEKGQLIQME
VERGYKTFLS RVAIGRDMSV EAVDSVGQGR VWLGAKAKEL GLVDELGGLE TAIRLAARLA
GLHEGYAVDY GTTSTSFLEE LFASKTSERF TARLRDFFMT DEEKKIREFF REGYRYTGIL
ARLPYEYTSY
//