ID I3DN89_HAEPH Unreviewed; 1505 AA.
AC I3DN89;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=IgA-specific serine endopeptidase {ECO:0000313|EMBL:EIJ73182.1};
DE EC=3.4.21.72 {ECO:0000313|EMBL:EIJ73182.1};
GN ORFNames=HMPREF1050_0324 {ECO:0000313|EMBL:EIJ73182.1};
OS Haemophilus parahaemolyticus HK385.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=1095744 {ECO:0000313|EMBL:EIJ73182.1, ECO:0000313|Proteomes:UP000003016};
RN [1] {ECO:0000313|EMBL:EIJ73182.1, ECO:0000313|Proteomes:UP000003016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HK385 {ECO:0000313|EMBL:EIJ73182.1,
RC ECO:0000313|Proteomes:UP000003016};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000256|ARBA:ARBA00004571}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004571}. Cell surface
CC {ECO:0000256|ARBA:ARBA00004241}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}. Periplasm
CC {ECO:0000256|ARBA:ARBA00004418}. Secreted
CC {ECO:0000256|ARBA:ARBA00004613}.
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:EIJ73182.1}.
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DR EMBL; AJSW01000007; EIJ73182.1; -; Genomic_DNA.
DR RefSeq; WP_005705508.1; NZ_UGHI01000002.1.
DR SMR; I3DN89; -.
DR GeneID; 78223489; -.
DR PATRIC; fig|1095744.4.peg.313; -.
DR OrthoDB; 8610050at2; -.
DR Proteomes; UP000003016; Unassembled WGS sequence.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd01343; PL1_Passenger_AT; 1.
DR Gene3D; 2.160.20.20; -; 1.
DR Gene3D; 2.40.10.120; -; 1.
DR Gene3D; 3.30.160.280; -; 1.
DR Gene3D; 2.40.128.130; Autotransporter beta-domain; 1.
DR InterPro; IPR005546; Autotransporte_beta.
DR InterPro; IPR036709; Autotransporte_beta_dom_sf.
DR InterPro; IPR012332; Autotransporter_pectin_lyase_C.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR000710; Peptidase_S6.
DR InterPro; IPR030396; Peptidase_S6_dom.
DR InterPro; IPR004899; Pertactin_central.
DR PANTHER; PTHR12338:SF10; ADHESION AND PENETRATION PROTEIN AUTOTRANSPORTER; 1.
DR PANTHER; PTHR12338; AUTOTRANSPORTER; 1.
DR Pfam; PF03797; Autotransporter; 1.
DR Pfam; PF02395; Peptidase_S6; 1.
DR Pfam; PF03212; Pertactin; 1.
DR PRINTS; PR00921; IGASERPTASE.
DR SMART; SM00869; Autotransporter; 1.
DR SUPFAM; SSF103515; Autotransporter; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR PROSITE; PS51208; AUTOTRANSPORTER; 1.
DR PROSITE; PS51691; PEPTIDASE_S6; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EIJ73182.1};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 26..285
FT /note="Peptidase S6"
FT /evidence="ECO:0000259|PROSITE:PS51691"
FT DOMAIN 1245..1505
FT /note="Autotransporter"
FT /evidence="ECO:0000259|PROSITE:PS51208"
FT COILED 973..1074
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1505 AA; 167930 MW; B0CECD0BF40E11BF CRC64;
MSKSNIFRPT FIALNVAVMC AGTQASMVRN DVDYQYFRDF AENKGQFFIG AKNIPIFDKQ
GKSVGTMLPN LPMPDLHVAS RVSGVATLFN PQYIASVKHN GGYGSVQFGE NSNNPDSHHF
DYLITDRNNH DKYDFHSPRL HKLVTEVTPI PLNNIAFDNN RKTGPKNGAF LDKERYPYFV
RVGSGRQYLR SKDGKEKTSL TSAYNYLTGG TPLKPNSSMD NWVLFSGDLY ETLGTYGLPG
DSGSALLAYD AKEQRWVLAG VLSTFNGYDG KNNIYTIIQP DSIHRAFEND EMTVSLNGST
YSWQNRGVGK SVLQSGNQAV EIPVTNVNVA SKDENRQRPS LDNGKTVHFT GRDGSTLVLK
ESINQGAGAL HFNQNAIVRT DSNDVTWLGA GVVVNGNKTV NWRVKNPKND RLSKLGTGTL
YVDGQGKNLG DISVGEGTVV LNQKSLNGQQ QAFNQVGITS GRGTVVLAND KQVNPDNIYF
GFRGGRLDVN GHNLTFHRIQ NSDDGARIVN NSRTQAAEIN IIGRDNFAQQ DIEWVNWGQH
PTTSLAIYEY KNNYRNNRLD YFRLKEGKNP RAYFPWDMET TNDWEFLGNN KSEVIQRVLA
EANARKHLDT YSGFLGETDQ RYHNGRLSIA YRPQVANSIL SLTGGTNLNG NIYVENGKLL
LSGVPVPHAY DHLNKKEVIE EGNWINRQFK ANEFDVAGNA ILESSRNVSV LEGNFNARHQ
AQIQLGFAQG KSDECIRESY SGTTKCSEKA VISQTVFNSV PVTSVYGDVS LEHQSQFSLG
KAHLMGRINS VGAETQVNLL PHSEWTLNNN SVVGNLFLAP NSQITLNSLY DEMSSTYKGW
VKFNQLVVDG QLTGNGHFRF LANLAESRGD NVVVNGLASG NYLLSLKNTG EEPKNVAPLS
LVKLNHPNQH RQNAHFALEN GFVDLGAYRY ILANFNNDYR LYNPLRDAEL HFGSNSELVA
NSQREFNVVH QALVDKEHEL ARLERSYTQA EGVNKIDQNR ASRLLEEIHN TTNSYNQATS
EYNRTARIRF IKRGRLYKQF TQLKVLLERQ RNEYRGLSEQ EKRSQQEVQK LLNLVNQTKT
DLHSIESRQD NVLEEMNRLQ AGLASSIARA QQLCEAQNLS SDICRKVAKV ANEGNVTLFE
EEIDASIERI ELAQQALANA QGNQGEKDIA QSSLNESVLA LLDSLNKAYQ TEQEIQQFLS
TQSGTVSIPV QSQLISRYSN TALSELSANV NGALQIGRNL DRHLSSGDPS NVWMNTESTK
QTYRSDYYRP YKQTMTLTQI GVAQDVSDNV KIGAVLSHSR ANNEFNENVS GKHRFTSVNA
FTKGNWENGI FASVDLGYGR SRNTVTFDGK DNVFHRNIFN VGGNLGANWD LSGWLNVQPS
IGVRYYRLSG VTYNLSEAKI ASKALRLTTY RVGVLLDKTF DINGVKVTPS FTINYYDATQ
HKLAIDGALS VNNVVMKQQF GRYFTHEVGL SAQFHRWNIS THIGMLKGSD VAPQKFGAVK
VGFTW
//
