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
//