ID C0ZAE0_BREBN Unreviewed; 2580 AA.
AC C0ZAE0;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Putative extracellular serine protease {ECO:0000313|EMBL:BAH42749.1};
DE EC=3.4.21.- {ECO:0000313|EMBL:BAH42749.1};
GN OrderedLocusNames=BBR47_17720 {ECO:0000313|EMBL:BAH42749.1};
OS Brevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=358681 {ECO:0000313|EMBL:BAH42749.1, ECO:0000313|Proteomes:UP000001877};
RN [1] {ECO:0000313|EMBL:BAH42749.1, ECO:0000313|Proteomes:UP000001877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=47 / JCM 6285 / NBRC 100599
RC {ECO:0000313|Proteomes:UP000001877};
RA Hosoyama A., Yamada R., Hongo Y., Terui Y., Ankai A., Masuyama W.,
RA Sekiguchi M., Takeda T., Asano K., Ohji S., Ichikawa N., Narita S.,
RA Aoki N., Miura H., Matsushita S., Sekigawa T., Yamagata H., Yoshikawa H.,
RA Udaka S., Tanikawa S., Fujita N.;
RT "Brevibacillus brevis strain 47, complete genome.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC ECO:0000256|RuleBase:RU003355}.
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DR EMBL; AP008955; BAH42749.1; -; Genomic_DNA.
DR RefSeq; WP_012685492.1; NC_012491.1.
DR STRING; 358681.BBR47_17720; -.
DR KEGG; bbe:BBR47_17720; -.
DR eggNOG; COG1404; Bacteria.
DR eggNOG; COG5492; Bacteria.
DR HOGENOM; CLU_000293_0_0_9; -.
DR Proteomes; UP000001877; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 1.
DR CDD; cd07477; Peptidases_S8_Subtilisin_subset; 1.
DR Gene3D; 2.60.40.1080; -; 7.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR003343; Big_2.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR008964; Invasin/intimin_cell_adhesion.
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; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR InterPro; IPR034202; Subtilisin_Carlsberg-like.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF02368; Big_2; 2.
DR Pfam; PF17957; Big_7; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SMART; SM00635; BID_2; 7.
DR SMART; SM00060; FN3; 2.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 5.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS50853; FN3; 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}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000001877};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..2580
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002905718"
FT DOMAIN 2162..2246
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT ACT_SITE 135
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 165
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 320
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 2580 AA; 278992 MW; 503ACC963D2338A8 CRC64;
MNSKFIRSIS ICNVFILLSL LFLQAVPEQV RATEKSKTYL IGFKDSKRTK RSAIQGTSVQ
QLSSKIMVAT LTESEREELS QDRNVAYIEE DSDTELAEID LTEKQEIPWG VEHVGALQAH
SKNYLGKNVK IGILDTGISR HEDLKVNGGI SYVEGEVDYD DAHGHGTAVA GVIAGKDNHL
GIVGVAPEAE IYSIKVLDEK GHGKYSSMIQ GIEWAIQNGM NIISISAGGS VGSQALHDQI
KRANEHGILV IAAAGNRGLG EDTQLFPAHY PEALSVGSVD RDNQRADTSS VGAGLDLMAP
GVDILSTSLH KGYELRSGTS LAAPHVAGAA AVIWSKKGKA TSDEVRDILI ESATPLGEPR
FYGKGLVNLE KALEIGSTQS TGIQAIESNP NELAISVGQS HPLKIKAKLK DDTTKDITEQ
ANYASNDEKI ATVNPTGMVI ATGIGETRLI VTFEDKTIEI PVVVSEKVPL TPRGGLDTPE
NGEFIVSTYV LKGWYLDPAG VSQISIMVDG LKVGEATYGD PRPDIEAKYP AYQNGNAGFH
FNLDTREMSV GLHTISLAIQ NKNGEQSVIE GNTFYVGTKQ PVEGLHADVS KLELTDENTH
QLVISTILED KTLKDVTMLA EYTSSDESIV TVSPTGFVKA KGLGTAIVTI RYEGQAITLP
VTIQEKIALI PRWELESPAD HSTMTGVSLM KGWYLDPAGV AKIAVHVDGK LVGEALYGQS
RPDIAQEYPA YQNATSGFQY FLDTTQMTEG QHTITLMAVN QEGKEQVLAE RSVSIERAQP
AKSIAANVSK VELSQGNTQQ LTISAVLQND QIRDVTREAK YTLEDSTVAS ISDHGIITGL
QIGKTTVIVD YQGQVLTLPI TVKAAAGASQ GGLDSPLDNA TISGIYPVTG WFIASSGVSS
IEVLVDGVVI GEAKYGVPRP EIEITDISLP GSNVGFQYSL DTALLQKGKH AISVRGTAKD
GNQTMLGSRT VQVVELIPAI GLHVDIAELQ LSQGKTHPLT VKAELKDQSK QDVTKLALYT
VENPSVAKVS PDGVVTALAQ GNTSLTIKYG NQSIQIPVVI TAAEVRKAIG EIETPANDAV
IHGSYTIAGW FLHPSTPTRY QVFLDGKEVG QANSGIARPD IALLHPDYKN AHAGFSYTMD
LSDLQSGHHT VSVVVTDSEG KQYPLPEKSF VVREITPADS LKHTESGISL AKSSMQKLRI
TATTAGQSPK DVTAHAVYSY ENANVIHVSP LGIVTGLEVG MTKIVVSYGG QTLTIPVVVT
ETESGPLVAK GKIDIPMEKA EIGGTTTIQG WLLDPDGVAK IEVWMDGQLQ GTAVYGGPRP
DIFALYPRYE NANAGFQYQL HTMSFNEGEH KITVRVTNKK GVESLVLDKE VTVGPVTGIT
TNLSTIDLEK EKTASLTVVA AYRDKSTKDV TGEATYAIQD PAIAKIDETG VITGLAPGNT
VLSITFAGIV QQVPIHVKGG TLTTTGAIDA PEENEQISGS YNVAGWFMTS GEVEKIEVQM
DGVALGEAKY GLERPDILRM YPEAPPVKPG FSYLLEVNDL DLGQHQLTVL VTEKDGKQTS
MEKAITIVKP IHDKYTYWLQ FSDQQGKDNW SYQEVSGNQH ADLTWNKQTE EWKGNHDTAI
GNTWIKVGST SPVIKWEAPR SGKIQVSGWI SKIQVDEGDG VNVRLLKNDE QIWPSTGWQA
IEFNDEIGVG LQEELEVEQG DALLFQVDQK ESSIGDLLKW TPEITYVSNA VNDNASPQIY
LTSPVVGAAV STVDGKDVVA ISGFAMDPNM GDQVNIWYQL DDGDPQELTR FTASEKPQPF
LFNLPTHHLK PDVLYSLRVW AVDQKSGRSL SEKVDFTLDM IAQAEKEDIV VVADWKSPKD
GTEISKGEKV SLTWEYVGYG GHSSKIESQE LLIYISEGGR VTSTIREKLT GTARSYVFDT
SVIEKNARVE ARIRTIMPKT PAYVYGGTAK LNFSVLAANQ APVVASTGFV TLDRGLTGTI
NYTLNENDVT DKIVSTKLRV GFTPGGNEIV EKEELIPEAS QNRQVVSRYS FPLTKDMLHQ
TIYWTVQAQD NRGAWTPAVN YSVPLEEALP KIVIYTPVAK RVMDLDDIFT LDGTYTKLTS
GETIEAKVSS SHSAKKFTTT GTSGQWELNW TGRELGSGTY ENIQVTEPIV AYYSGSLTVE
DKPDAPSIVN VEAETNSLKI YWSPSVGAID YGVQVDGGGI KKVGDVTNHT IAGLQPSRVY
TIKLWAYTST GISSYSSSIT VETRPAEGNF NGMVENSPVR MYFPANEAQY MKIVAGANGT
YSFTLNNDSG SPANATLSVY KAASLQAHEE IAADANGRVN PVFVAGKTYY VKIVAKDSIY
ATLLAKPGGE AFTFNQPKEI TLQPGQTVEM AMNTIISGKY RMTTQLKNQT HKYPVVTVLS
NGNAITPKET PTPSESNYEL GMGNYTIKLT NTESYPVSVS FTVFAPPPGG TLYEYVYDQN
NRIKAIKENG VESVTFIHDE NGNILKSVKH AVTLPPKGTV LHVDQEKVEV RAGSTRPIKV
TATKEDGSTL DVTTQGLYTV VDSRVGFIVK GVVYGMNPGT TEARVSYDGQ FKTITITVVP
//
