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Database: UniProt
Entry: A0A098F477_9BACI
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ID   A0A098F477_9BACI        Unreviewed;      1359 AA.
AC   A0A098F477;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=Peptidase Vpr {ECO:0000313|EMBL:CEG29424.1};
GN   Name=vpr_3 {ECO:0000313|EMBL:CEG29424.1};
GN   ORFNames=BN1002_04362 {ECO:0000313|EMBL:CEG29424.1};
OS   Bacillus sp. B-jedd.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1476857 {ECO:0000313|EMBL:CEG29424.1, ECO:0000313|Proteomes:UP000042335};
RN   [1] {ECO:0000313|EMBL:CEG29424.1, ECO:0000313|Proteomes:UP000042335}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-jedd {ECO:0000313|EMBL:CEG29424.1,
RC   ECO:0000313|Proteomes:UP000042335};
RA   Urmite Genomes Urmite Genomes;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; CCXR01000001; CEG29424.1; -; Genomic_DNA.
DR   RefSeq; WP_048827473.1; NZ_CCXR01000001.1.
DR   STRING; 1476857.BN1002_04362; -.
DR   OrthoDB; 9798386at2; -.
DR   Proteomes; UP000042335; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd14254; Dockerin_II; 1.
DR   CDD; cd02133; PA_C5a_like; 1.
DR   CDD; cd07474; Peptidases_S8_subtilisin_Vpr-like; 1.
DR   Gene3D; 2.60.40.4130; -; 1.
DR   Gene3D; 3.50.30.30; -; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 2.
DR   InterPro; IPR002105; Dockerin_1_rpt.
DR   InterPro; IPR016134; Dockerin_dom.
DR   InterPro; IPR036439; Dockerin_dom_sf.
DR   InterPro; IPR046450; PA_dom_sf.
DR   InterPro; IPR003137; PA_domain.
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; IPR034213; S8_Vpr-like.
DR   InterPro; IPR010259; S8pro/Inhibitor_I9.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   PANTHER; PTHR43806:SF65; SERINE PROTEASE APRX; 1.
DR   Pfam; PF00404; Dockerin_1; 1.
DR   Pfam; PF05922; Inhibitor_I9; 1.
DR   Pfam; PF02225; PA; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52025; PA domain; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   SUPFAM; SSF63446; Type I dockerin domain; 1.
DR   PROSITE; PS51766; DOCKERIN; 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   Cell wall {ECO:0000256|ARBA:ARBA00022512};
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:UP000042335};
KW   Secreted {ECO:0000256|ARBA:ARBA00022512};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}.
FT   DOMAIN          1274..1338
FT                   /note="Dockerin"
FT                   /evidence="ECO:0000259|PROSITE:PS51766"
FT   ACT_SITE        229
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        282
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        601
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   1359 AA;  148371 MW;  2FEF5BD43E8571B6 CRC64;
     MKSKSFFKQA AVVTLSVGLI LSSTNFNFAP KASAASSKAE SILASLTPEQ RNALKQLELT
     EQTGLRGFNK QELNSEKEVD VIVQFHSKPG KIAVLDAEVK GKKLSKEKAD ERVAREHEKF
     KKDIQSILSS GNIKGKQANH TITSSYNTVY NGVTVKLPAN QVVNLLKSDV VKAVYKNETY
     KVDPIVPAGD GDKESSTPGT SVESLSHLKV DKLREEGLTG KGVKVGVIDT GIDYNHPDLQ
     KVYKGGYDFV DKDNDPMETT YEDWKKTKYP EVNNGSAYYT SHGTHVSGTI AGQGTNKDIS
     VEGVAPEVDL YAYRVLGPYG TGTANNIIAA VEKAVEDGMD IINLSLGSGI NDPYYPTSTV
     VNNAVLSGVT AVVAAGNAGP GEYTLGSPGA AALALTIGAS DVPMTVSTFK GQIGSVSDIK
     LVSMARHYLD KLKELEGRSL QVVDVGIGAN ADYNGKEVQG KAVLIARGEI ALHDKVALAK
     QKGTAAVLLS NNVEGQINAN LGESTLYIPT FSVAKDAGEK IKAQLQAGQT GFTFSGYGVS
     QTEGDHLADF SSRGPVRQTY GMKPEVVAPG VSVLSTVPYY IANPKDQGNY QFAYSRFSGT
     SMATPFTAGV AALMLQANPK LEPEDIKTVL MNTANPLNGN YSIFEAGAGI VNPYKAVHHG
     ASFQVLDKTL IPGAENLVEV KSLTGGLSFN HELVDTNLQI TKSIKVKNNE KMKKMFSVDI
     TEGKGSNSLK QNGMKINLAN KITINGNEEK TITAKLLSHK KAKEGYYTGY ITFTNTENSA
     EQYRLPFSFR LLEEGFNKIE IDNPVFSPGY LNEEPLDYFR EPYVYSQLNI KAPMEKLDVI
     LQDEKGNDLG LIGTANLNGA YDSVTYGLTF FNGLYYKFTG DPEKPISSRY SFAQEGHYKI
     KFIGTGQSGK TFYETRHLWI YLNQPNFDSS LDGASPFIEY KPGQATYPFE IRITDPIVDE
     VKKYGLNYDQ SSNYMVYYWG PWGGFPSTPI YMDKDGRFVE EVAMKESEKV LYFRMDGYNT
     AGNKINKDYY FVKEGTPVTY PTSDTTEVNT GGTIKATIML DNVQDIAKAD WNFNDSFGFK
     NLEVVDAKLA DAFVDKAKID LKGDHVTVEF HQPSDEFDQQ AVAEVTIKVS DDLFFTQGTI
     NPTVAVTDGD NKMIRVFNAP YTFKINPQFS VVEGTIGPEG FFIGDPEWDG YLSKKDWTKV
     GGSVKLMDSN GQVYDATSSI DPYGKFNSKK LPVSQEPYIL EMKAPGHFLT KVEAPGAIIK
     DGKANAINFN LYMTLLTAGD VNQDGAIDVL DALAVQKVWK TADRAADINF DGVVDEKDMA
     FVQKNYLKQN QDVENAPEPK KNADGKTLEM ILAELGIGS
//
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