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Database: UniProt
Entry: D8J199_HERSS
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Original site: D8J199_HERSS 
ID   D8J199_HERSS            Unreviewed;      1371 AA.
AC   D8J199;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   02-APR-2025, entry version 66.
DE   SubName: Full=Serine endopeptidase protein {ECO:0000313|EMBL:ADJ64668.1};
DE            EC=3.4.21.- {ECO:0000313|EMBL:ADJ64668.1};
GN   OrderedLocusNames=Hsero_3186 {ECO:0000313|EMBL:ADJ64668.1};
OS   Herbaspirillum seropedicae (strain SmR1).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC   Burkholderiales; Oxalobacteraceae; Herbaspirillum.
OX   NCBI_TaxID=757424 {ECO:0000313|EMBL:ADJ64668.1, ECO:0000313|Proteomes:UP000000329};
RN   [1] {ECO:0000313|EMBL:ADJ64668.1, ECO:0000313|Proteomes:UP000000329}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SmR1 {ECO:0000313|EMBL:ADJ64668.1,
RC   ECO:0000313|Proteomes:UP000000329};
RA   Pedrosa F.O., Monteiro R.A., Wassem R., Cruz L.M., Ayub R.A., Colauto N.B.,
RA   Fernandez M.A., Fungaro M.H.P., Grisard E.C., Hungria M., Madeira H.M.F.,
RA   Nodari R.O., Osaku C.A., Petzl-Erler M.L., Terenzi H., Vieira L.G.E.,
RA   Almeida M.I.M., Alves L.R., Arantes O.M.N., Balsanelli E., Barcellos F.G.,
RA   Baura V.A., Binde D.R., Campo R.J., Chubatsu L.S., Chueire L.M.O.,
RA   Ciferri R.R., Correa L.C., da Conceicao Silva J.L., Dabul A.N.G.,
RA   Dambros B.P., Faoro H., Favetti A., Friedermann G., Furlaneto M.C.,
RA   Gasques L.S., Gimenes C.C.T., Gioppo N.M.R., Glienke-Blanco C., Godoy L.P.,
RA   Guerra M.P., Karp S., Kava-Cordeiro V., Margarido V.P., Mathioni S.M.,
RA   Menck-Soares M.A., Murace N.K., Nicolas M.F., Oliveira C.E.C.,
RA   Pagnan N.A.B., Pamphile J.A., Patussi E.V., Pereira L.F.P.,
RA   Pereira-Ferrari L., Pinto F.G.S., Precoma C., Prioli A.J., Prioli S.M.A.P.,
RA   Raittz R.T., Ramos H.J.O., Ribeiro E.M.S.F., Rigo L.U., Rocha C.L.M.S.C.,
RA   Rocha S.N., Santos K., Satori D., Silva A.G., Simao R.C.G., Soares M.A.M.,
RA   Souza E.M., Steffens M.B.R., Steindel M., Tadra-Sfeir M.Z., Takahashi E.K.,
RA   Torres R.A., Valle J.S., Vernal J.I., Vilas-Boas L.A., Watanabe M.A.E.,
RA   Weiss V.A., Yates M.A., Souza E.M.;
RT   "The genome of Herbaspirillum seropedicae SmR1, an endophytic, nitrogen-
RT   fixing, plant-growth promoting beta-Proteobacteria.";
RL   Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR   EMBL; CP002039; ADJ64668.1; -; Genomic_DNA.
DR   RefSeq; WP_013235132.1; NC_014323.1.
DR   STRING; 757424.Hsero_3186; -.
DR   GeneID; 29391865; -.
DR   KEGG; hse:Hsero_3186; -.
DR   eggNOG; COG1404; Bacteria.
DR   eggNOG; COG3266; Bacteria.
DR   eggNOG; COG4625; Bacteria.
DR   HOGENOM; CLU_256268_0_0_4; -.
DR   OrthoDB; 5760545at2; -.
DR   Proteomes; UP000000329; Chromosome.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04848; Peptidases_S8_Autotransporter_serine_protease_like; 1.
DR   Gene3D; 2.40.128.130; Autotransporter beta-domain; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR005546; Autotransporte_beta.
DR   InterPro; IPR036709; Autotransporte_beta_dom_sf.
DR   InterPro; IPR013425; Autotrns_rpt.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR050131; Peptidase_S8_subtilisin-like.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR034061; Peptidases_S8_Autotransporter.
DR   NCBIfam; TIGR02601; autotrns_rpt; 2.
DR   PANTHER; PTHR43806:SF11; CEREVISIN-RELATED; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   Pfam; PF03797; Autotransporter; 1.
DR   Pfam; PF12951; PATR; 2.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SMART; SM00869; Autotransporter; 1.
DR   SUPFAM; SSF103515; Autotransporter; 1.
DR   SUPFAM; SSF51126; Pectin lyase-like; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51208; AUTOTRANSPORTER; 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:UP000000329};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          1091..1371
FT                   /note="Autotransporter"
FT                   /evidence="ECO:0000259|PROSITE:PS51208"
FT   REGION          838..907
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          950..976
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        838..855
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        863..900
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        99
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        156
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        349
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   1371 AA;  138605 MW;  FB02D3A65691632F CRC64;
     MKKSRKSPQN AALTTSAVFR KQGLYAAVLL TLGPALGTPA SAQSYVNYDG ASTADASAAL
     ATWTGHAEFK ADWGLGAMNA QYAYVAGYTG QGIKLGAVDS GLLLTHNEFA RRNVKALAVT
     GAYANDGYQY QDGSQAWKAG DAFSVPGALS PLNDKHGSHV SGTIAAAKNG DGIMGVAFAS
     DYYITNTNGT DSSVYGVNMD YNYFKAAYGN LASAGVRAIN SSWGNPDSRD DFGSISGVAA
     AYQRLQGGGK KSWLDAAADV AQASNTLLVW AAGNASKANV NIRSALPYFR PELEQNWIAV
     AALNTSSMLP SFSNQCGLAK YWCVSAPGSG ITSLNITSDT ALVNASGTSM AAPHVTGALG
     VLMQRYPDLD NQAIRTILLS TAKHLGTGAA DAPNSMFGWG VPDLNKALYG PGQLLGVFKA
     NIAAGSTDTW SNDISEAALV QRKSEDKAQL AAWQALSAST LQSAVDSASA QVKAQVDSGY
     DAALALVQTR AQLNAAYQSS NKREDKTAFQ NADKAVAANA LAAAILKQSG SGALLSKDQL
     LAYMLTVDSG VAAANLALGN YNGQAVYLAA AQKKTDADYV GSLVKTGDGS LTLSGNNSYT
     GGTRLEGGTL GVGSSTALGT GGLAMSDGVT LRAAADNLAL NNAVSINGAG RIDTQAFNLT
     LNNGIADGRV PGSLVKQGEG TLRVLGTVSY SGNTTIAAGT LSLPTYVQTA GQILTVGVAS
     ATQYGKLAVT GAASFASDAA LAVDVAKAAT LGNGQRLAGV ITAGSLSAPR LAVSDNSVLF
     DFQPVVASNA VDLDIVSAVS INKVVLDTLA QAQGPANTAT TSTPVASALA SSTPVASTPV
     VSAPASNTPA ASTPVVSVPA SNTPAASTPV VSAPASNTPA ASTPVVSAPA SNTPAASTPV
     VSVPASNTSA ASTPLVSVPV SNTPAASTPV VSVPVSNTPV ASTPVVSVPA SNTPAASTPV
     ASAPASGTPA SSTAAPSASA APAVVPAVAP AARIPSVVAA ATAAATVAPI LDRQIQQPSS
     ADMAQVVTAL GRLPDAASVL RAASQTLPRN VSDNAIRGVL ASLDRVIATR LDLGNLAGSA
     TGTGSGLGYG EAGGDRQVWL MPFESRTNQG DRDGDSGFSA STWGMATGAE MAWDSGRVGL
     SYAYASTSAS GNTAITGAGS RSRIESNLVA LYGSVPLGKL ALSWQADAGW NSNRLAREMQ
     FGGLHRIASS RYHTWSAHLG ANVSHTLPLS EALSVVPALQ LDYTRMQSPS YAESGAGDLS
     LSVQGKRTQA LLLGVGTRLN YALSTTSQIS THVGASYDVI NDRGDLVATY AGTPGQAFTA
     PGSARSAWLF KAGVSYRFQL TTEADISLRL DAEGRSGFIN QSAALKASWR F
//
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