ID A0A0Q0HWQ3_9GAMM Unreviewed; 1277 AA.
AC A0A0Q0HWQ3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Minor extracellular protease vpr {ECO:0000313|EMBL:KPZ69102.1};
DE EC=3.4.21.- {ECO:0000313|EMBL:KPZ69102.1};
GN Name=vpr_2 {ECO:0000313|EMBL:KPZ69102.1};
GN ORFNames=AN944_03118 {ECO:0000313|EMBL:KPZ69102.1};
OS Shewanella sp. P1-14-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=1723761 {ECO:0000313|EMBL:KPZ69102.1, ECO:0000313|Proteomes:UP000050414};
RN [1] {ECO:0000313|EMBL:KPZ69102.1, ECO:0000313|Proteomes:UP000050414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1-14-1 {ECO:0000313|EMBL:KPZ69102.1,
RC ECO:0000313|Proteomes:UP000050414};
RA Gilbert D.G.;
RL Submitted (OCT-2015) 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 -!- 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:KPZ69102.1}.
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DR EMBL; LKTL01000021; KPZ69102.1; -; Genomic_DNA.
DR RefSeq; WP_055025530.1; NZ_LKTL01000021.1.
DR AlphaFoldDB; A0A0Q0HWQ3; -.
DR PATRIC; fig|1723761.3.peg.3195; -.
DR Proteomes; UP000050414; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02120; PA_subtilisin_like; 1.
DR CDD; cd04852; Peptidases_S8_3; 1.
DR Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
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; IPR013783; Ig-like_fold.
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; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034197; Peptidases_S8_3.
DR InterPro; IPR010259; S8pro/Inhibitor_I9.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR InterPro; IPR045051; SBT.
DR PANTHER; PTHR10795; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 1.
DR PANTHER; PTHR10795:SF468; SUBTILISIN-LIKE PROTEASE SBT3.18; 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 PROSITE; PS51892; SUBTILASE; 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:UP000050414};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1277
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006180992"
FT DOMAIN 112..162
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 194..647
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 454..526
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT ACT_SITE 203
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 277
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 611
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1277 AA; 134096 MW; 469BE8DF1C1B4A13 CRC64;
MTSIYKKSLI AAALTLAFSP NLQAKVIDTR GLDTDSGQRG YQPTTKNPRQ IDNLYMVLLD
DQPLATYHGD KGDLKATSIL ANPSNSRAKT GVLNVNSAVS QQYIQYLNTQ RSKTLSLAKS
TLNRQLAVHD DYQIALNGFS TELSEKEAQM LASVAGVKSV QKVELRHLNT DSGPKHIQAP
SAWDGSATGV SSMGEGVIVA IMDTGINHTS ASFADIGGDG YDHTNPLGEG TYLGHCSDSD
LAHYCNDKLI GIWAHEALLD DYTPEGDDRI GIDHNGHGSH VASTTAGNIV KDVTVYNAVG
EEAEFSFGQI SGVAPHANIV SYQVCAADAG CWPDVTALAV EHAIEHGVQV INYSVGGGAS
DPWNDTDALA FLAAREAGIH VAVAAGNDGP GAETVGSPGN APWLTTVAAY THDRSFTDKE
VTFTGGDYDL EPLTGKGATS GISGDIISAA DLGMAGCLEP FDADTVTGKI VVCERGDIAR
VAKGTNVRAG GAAGLVLINL EGGAETVDAD LHVLPAVHLD ADQGALLTDW LSSGSDHTVS
FNASVLESDP AKADIAAEFT SRGPESIMNR WLTPHISAPG VEIYGANTEY QPWRDTGDKT
ESPTTFMSGT SMASPHIAGV YTLIAALKPE WTPAQAQSAL MLSAETNTWM EDGVTPSSLF
TGGAGSARVA DALNAGLVMD VSHEDYTLAD PSLDGTPESL NLPSALMNNC MMACSWTRTF
TATASSTWTV GELSQTPGLS ISATPSSFTL AAGESISLDI TAAIGEGYAS EYGMGYLVLT
PENTALTPTK MPVVGSFVAG SMPEIAQLTT GQNKGSAAIS GIKTVGSSDI QVGVFELAEV
EVIETTIPRD DSDTSNWPTN VYNDSSKYYS QLVNITPNTK RLIARVKHTS SPDLDLYIGR
DSNYNGKPDN AREMDPLTCM SATETAYESC EINDPDPGSY YVTVHNYGDT SAPSDVEDDV
VIELAVIGKD DESVTVDFKS AVAADEDIGL VLNWDKTLKS DTLYTTVLEI GTGVDAADNV
GLMPIELYRK ATYAQSQLDV ESADTGDMIT LSIALADNDT DEERTLSVTA QLPVGLVIES
DSHQGSVDGE MVSWEVVQAA NEAGQEIVVE LDTQALVMSQ DLVFSVSHTL NEVSHTEMLA
PVMLSGVPVA KINGEQSISL TVDEGTTVSL SASDSTAPNS DDELTYAWSQ VSGPVVTFAD
AMAMDTDVTL PAVDADASAV IELTVSNGVK TAVAATATIA VTAEVIAPEP EPKSDSSGGA
MGLWLFVLGL LGLRRRS
//
