ID K6YNK8_9ALTE Unreviewed; 1049 AA.
AC K6YNK8;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Cucumisin {ECO:0000313|EMBL:GAC12915.1};
GN ORFNames=GLIP_0261 {ECO:0000313|EMBL:GAC12915.1};
OS Aliiglaciecola lipolytica E3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Aliiglaciecola.
OX NCBI_TaxID=1127673 {ECO:0000313|EMBL:GAC12915.1, ECO:0000313|Proteomes:UP000006334};
RN [1] {ECO:0000313|EMBL:GAC12915.1, ECO:0000313|Proteomes:UP000006334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E3 {ECO:0000313|EMBL:GAC12915.1,
RC ECO:0000313|Proteomes:UP000006334};
RX PubMed=25009843;
RA Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT high degree of genomic diversity and genomic characteristic for cold
RT adaptation.";
RL Environ. Microbiol. 16:1642-1653(2014).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC ECO:0000256|RuleBase:RU003355}.
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:GAC12915.1}.
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DR EMBL; BAEN01000011; GAC12915.1; -; Genomic_DNA.
DR RefSeq; WP_008842735.1; NZ_BAEN01000011.1.
DR AlphaFoldDB; K6YNK8; -.
DR STRING; 1127673.GLIP_0261; -.
DR eggNOG; COG1404; Bacteria.
DR OrthoDB; 614750at2; -.
DR Proteomes; UP000006334; 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; cd04818; PA_subtilisin_1; 1.
DR CDD; cd04852; Peptidases_S8_3; 1.
DR Gene3D; 2.60.40.2310; -; 1.
DR Gene3D; 3.50.30.30; -; 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; 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; 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 InterPro; IPR041469; Subtilisin-like_FN3.
DR PANTHER; PTHR10795; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 1.
DR PANTHER; PTHR10795:SF468; SUBTILISIN-LIKE PROTEASE SBT3.18; 1.
DR Pfam; PF17766; fn3_6; 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; PS00136; SUBTILASE_ASP; 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:UP000006334};
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..1049
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003900208"
FT DOMAIN 49..150
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 174..648
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 427..512
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 704..810
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT ACT_SITE 183
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 258
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 594
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1049 AA; 110018 MW; 1676CD774896B07D CRC64;
MLRKQLTVLG TGCFLAMSVH SALALSNPDR SFVTADGSTS QTSASKTRYI VQLRGAPAAN
RPLKTNLPNK AGGILKSAKY DANSASNIAY RKELVNKQNK IMNDVGIKEA VYTYEHSFNG
FAANLTSAQV SKLRTNSEVI NIWPDEIREM DTSNTPSFLG LTSPDGLHTL GNKGEDMIIG
VVDSGVWPEN PSLDDTGFAP IQDTRPEWPN KEDVCDVGTD PLFECNNKLI GARYFNTGFG
PESLLPGEFD SPRDADGHGT HTMTTAGGNE SVSASILGVD VGLVTGMAPR ARVAAYKVCW
NGSAPGNSGC ATTDSVAAID AAVADGVDVI NFSISGSRTD LVDPVHVAFF NAARGGVFSS
LSAGNSGPGA QTVAHNVPWV TTVAASTYDG DTALIGNTLE VSYDDVTDDL YSVHGSITAP
VPEEGLSGQL VAATPALACD DGLTNPAEIA GNIALIARGV CNFSIKILNA QNAGATGVVV
YSDNRAPTPM GGDATGITIP GVMITNEKGL ELAGLVDEVT VSVNMTYDAI SGGTSTEIGN
QIAGFSSRGE SLATADIIKP DITAPGQQIL AGTSGSQIDS GLMGESYAYL SGTSMSSPHI
AGLAALVREA NPTWSPAAVK SAIMTTARQN LTKEDGATAA DPFDYGAGHV DPNFAVDPGL
VYDANEFDYW AFLCGQGESA FTESTSGFSC AAFENAGYPT DASDLNIASI AIDELAGTQT
ITRYVNNVSD LNSYVASVEA PSGIDVTVSV LDWNTGTFVD SDVMGFRESD GLGLYQLTFS
KNADVELNEW TFGSITWSDG THNVRSPIAI MPTEPVRVTA PDEINLVTTG SAARVTLSAE
VGYNGRFYAQ GIGLDTSTID EETGLGQVYG ESHVVSQDPD STFAFLEPGL AVYMVDVPEG
TRIAKFEINT DDLPNPAMDL DLYVWECPQF SCSQVGASTN FDSDETVTLV DPTPLANLGG
FDTYLVFVHG WDMAGEGPTE VPLHVWTVDE SGTTGLTVRA SSRAVAGRTS RVYVGMYGLQ
AGENYVGGVI YKDENGNENG LTVIDVEAQ
//
