ID A0A0N8KBR4_9GAMM Unreviewed; 1331 AA.
AC A0A0N8KBR4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=S8 family protease {ECO:0000313|EMBL:KPQ03666.1};
GN ORFNames=HLUCCO02_01575 {ECO:0000313|EMBL:KPQ03666.1};
OS Idiomarinaceae bacterium HL-53.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae.
OX NCBI_TaxID=1298881 {ECO:0000313|EMBL:KPQ03666.1, ECO:0000313|Proteomes:UP000053932};
RN [1] {ECO:0000313|EMBL:KPQ03666.1, ECO:0000313|Proteomes:UP000053932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL-53 {ECO:0000313|EMBL:KPQ03666.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC 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:KPQ03666.1}.
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DR EMBL; LIHO01000009; KPQ03666.1; -; Genomic_DNA.
DR STRING; 1298881.Ga0003345_1687; -.
DR PATRIC; fig|1298881.4.peg.294; -.
DR OrthoDB; 614750at2; -.
DR Proteomes; UP000053932; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04818; PA_subtilisin_1; 1.
DR Gene3D; 2.60.40.3440; -; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 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; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR045051; SBT.
DR InterPro; IPR017312; Subtilisin_Alteromonadales.
DR PANTHER; PTHR10795; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 1.
DR PANTHER; PTHR10795:SF468; SUBTILISIN-LIKE PROTEASE SBT3.18; 1.
DR Pfam; PF17963; Big_9; 2.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PIRSF; PIRSF037898; Subtilisin_rel_Sputw3181_3341; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 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}; Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..1331
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010197612"
FT TRANSMEM 1306..1325
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 200..648
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 448..536
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT ACT_SITE 209
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 274
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 608
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1331 AA; 138443 MW; 2C2DF976E4F0C035 CRC64;
MKTNQTRVPR MTLVASVVAS ALSFGVSASA LSPVQTELNA VLVGQGNSAE KATAQVQQQF
PTYYIIELED APLATYQGGV RGLAPTYRGA YGEEKLNLRS AAAQGYQAYL ADRQREFASE
LSNRFPSAQI ERNLNILLNG AVISIPGQVD AKNELLQIPG VKRVYEHELV YAQTDTSLEL
VNAPEVWELI GGDDARARAG DGVKVAIVDG GIRSEHPMFQ DSGHTLPSGL PDDDYCSVID
ASFCNDKLAV ARYYTPTFAV HPSEHISPLD YGGHGTHVAG TAVGNVVSTT YQGVDVGLSG
VAPGATLMVY KALFQTPAGT GSGSNAMLVP ALEDAVADGA DIVNNSWGGG AGGDPANSVY
TPIFEAAEAA GVLMVTAAGN SGNGPQTVGC PACAEPGLAV ANTQTGRFFA DKTVDGPGLD
GVPAIMGAGD FTWPTEDDGT GTQVEVAVEG PLMYSGAIDD TNVEGCAAFP EDSLLDHIAV
IPRGTCAFTD KAVNAENAGA IGLIVVDNAA TGIISMSMPG ANIPSVAISS SDGESLLASW
QEGDTGVISP EAQVFIDEAS TDIMSASSSR GPNGNASFLK PDVAAPGTNI LSAYAPRGGE
YNAISGTSMA SPHVAGAAAL LKQLNPDLNA LELKSLLMTS SNQDVLKEDA ATDATPFDRG
AGRLDIAEAV RSVLTFDKAS IASVGCAVSC EFERTVTNHL PTEGTWVGRV EFANAGVTGE
LSAEEVTIEG EGEATFTLAV DVSYANPGWV FGQVVWEDTS GQYADAHLPI AIMAQRTADS
AVLATTVTDA ANLTTDAPAA ISSRLGASGA SLPVSFTMMV PQGTEIDPES ITITSARANE
VGFSIAQNQR SMTWAGSVTD EAPTTELPVQ NFLATGTSLL DISPTSPSLP CTAGCDEILF
TFNVGNFGGF EWGGQPVNTI GLTENGLITA GDTSFSESFQ NQEMPNAESP NGALAPFWAD
FEVGGDNGGA IHYNVLSDGT NDWFVYEWND VARWNDPDGD RYTFAVWINL GTNQVFFNYV
DMPATLGTGS VGFENTTGEI GLSAYYNGSG FSPVSNSSHE AILAQGETGF IQFDYEVTPT
SIGTADDLDI TVLENESIAV DMSTVFELGL RTLSETRLDS DVGEWRAVQP MNFAAVGDGS
IEIVSAPVNG TIAAAEVAEG EEADPFAFVY TPEADFVGSD SFTYRVVDAN GLGTSTATVS
VIVENSNTAP TASATAPASA AFNTGVTLNG SASSDPEGDT LTFEWAQLSG PNVTLSNANA
ASASFTVPAL ATQGTAVFEL TVSDGEFSDS TTVSVTLERK PSSDKWYEGH FGGLLLLLAF
PLLFVRRRRK A
//
