ID A0A0P7ZJI2_9GAMM Unreviewed; 1212 AA.
AC A0A0P7ZJI2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Subtilase family serine protease {ECO:0000313|EMBL:KPQ02295.1};
GN ORFNames=HLUCCO02_06370 {ECO:0000313|EMBL:KPQ02295.1};
OS Idiomarinaceae bacterium HL-53.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae.
OX NCBI_TaxID=1298881 {ECO:0000313|EMBL:KPQ02295.1, ECO:0000313|Proteomes:UP000053932};
RN [1] {ECO:0000313|EMBL:KPQ02295.1, ECO:0000313|Proteomes:UP000053932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL-53 {ECO:0000313|EMBL:KPQ02295.1};
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:KPQ02295.1}.
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DR EMBL; LIHO01000012; KPQ02295.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7ZJI2; -.
DR STRING; 1298881.Ga0003345_1117; -.
DR PATRIC; fig|1298881.4.peg.1978; -.
DR Proteomes; UP000053932; 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; cd07474; Peptidases_S8_subtilisin_Vpr-like; 1.
DR Gene3D; 2.60.40.2810; -; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
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; IPR034213; S8_Vpr-like.
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; 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};
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}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1212
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010193890"
FT DOMAIN 192..639
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 427..513
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT ACT_SITE 201
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 266
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 586
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1212 AA; 127203 MW; 141F18A33C56A0C9 CRC64;
MSIPSKPRLL ATSISMALLV SYGVAADSSV QVERFERTEG DLTALKRDAR NPLRLQETEI
FIVQLKGEPL ATYAGAREQI GTLGAERSRP QLNLQSIQAR EHESFLHAQQ RSFVSDLQRR
IPRATMYRQF ATAMNAVAIE VPKGTSMQAL SAHPDVARVY RNELRYEQMD ASLDLINVAD
SWESAGGRAD AGAGVRIAIV DGGIRPENPM FTGAGLTPAT DRPADDYCAT VDASFCTNKI
IAARYSEPTI TINENEYMSP LDYGGHGTHV AGTAAGDIVD ANVSGTDVEL SGVAPGAYLM
VYKALFRTPA GPGSGSDVML VEALEHAIED GADVINNSWG GGPGANGTDS IYDVIFGNAE
DAGIVVVTAA GNDGPGEQTI GCPGCVEPGL TVAASATGRS FESRLSYDEL SLEIYPGSGN
FSISEDITAP LVLAENVSET DSLACEAFPA DSLEGTIVLV DRGTCSFEEK AGFAQAAGAV
AMVVANNEEG VIRMTMGAAT LPSVSVTQED GISLRNAYVE DSELTIGALT SVVELDDVNR
LADFSSRGQN GDNRYLKPDI TAPGVDILSA DSPDLVDAFG TKSGTSMASP HVAGAAALLR
QLRPELDARQ VKALLMGTAD GESVTNHNND DLADAFGQGA GLLNVGAAES ADFVLDSASL
VATTCQSSCA LERAVTNLSD EAIEVAVTTE NFSNPYVTAT VSSEGVETGD TASISVPAGE
SVTFSVTIDS RFADDGWNFG SLAVTSSAST QSFPIVFSSE RADDATVLNT EVVSGEPTWG
ELASVESRFE SPAKGEEVSV TVNFPEGFEV DNVAVSESNA SGTLEVGDTS ATWTGTFADP
SESSSITPIA APAGSVLDVA SGDLFVTPAG VGCAEETCDE FALLLEGLEG VGGLTYNGTT
YDSITVYDNG LIAIGDQSSV TSTYFNLDFP DAEVPNNIIA PLWSDFTMGG ELGGEVYYAG
VELNGVDYLV IEWHDAKVWT ETVSATDPSY TFSVWLGLGE SDDIIFNYVE VPAMPEFASI
GLEDLSGTVG LSYFFDGAGE TVSSDSALDV MLDIEPSEVL LSYDLPLAHS QNLTADTEWN
TEVAIDVLGS ATIVSERSLA TAIADVQGTE FNSRAPLIVE PTGAVNVVIR GVVEGGEVST
DGESITFTPD PTFKGEQVIT YVLADEAGNE SAEYTLTVNV APRDAKKWYE GNGGLFFLLL
LSAAAWRRAK RS
//
