ID A0A0A7EM66_9GAMM Unreviewed; 762 AA.
AC A0A0A7EM66;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Peptidase S8 {ECO:0000313|EMBL:AIY67141.1};
GN ORFNames=OM33_18915 {ECO:0000313|EMBL:AIY67141.1};
OS Pseudoalteromonas piratica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1348114 {ECO:0000313|EMBL:AIY67141.1, ECO:0000313|Proteomes:UP000030341};
RN [1] {ECO:0000313|EMBL:AIY67141.1, ECO:0000313|Proteomes:UP000030341}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OCN003 {ECO:0000313|EMBL:AIY67141.1,
RC ECO:0000313|Proteomes:UP000030341};
RA Beurmann S., Videau P., Ushijima B., Smith A.M., Aeby G.S., Callahan S.M.,
RA Belcaid M.;
RT "Complete Genome Sequence of Pseudoalteromonas sp. Strain OCN003 Isolated
RT from Kaneohe Bay, Oahu, Hawaii.";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
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; CP009889; AIY67141.1; -; Genomic_DNA.
DR RefSeq; WP_040135938.1; NZ_CP009889.1.
DR AlphaFoldDB; A0A0A7EM66; -.
DR STRING; 1348114.OM33_18915; -.
DR KEGG; pseo:OM33_18915; -.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_011263_15_3_6; -.
DR OrthoDB; 9790784at2; -.
DR Proteomes; UP000030341; Chromosome 2.
DR GO; GO:0046872; F:metal ion binding; 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; cd04817; PA_VapT_like; 1.
DR CDD; cd07477; Peptidases_S8_Subtilisin_subset; 1.
DR Gene3D; 2.60.120.380; -; 2.
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; IPR003137; PA_domain.
DR InterPro; IPR007280; Peptidase_C_arc/bac.
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; IPR010259; S8pro/Inhibitor_I9.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR InterPro; IPR034202; Subtilisin_Carlsberg-like.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF00082; Peptidase_S8; 2.
DR Pfam; PF04151; PPC; 2.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF89260; Collagen-binding domain; 2.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000030341};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..762
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002028431"
FT DOMAIN 49..123
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 149..353
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 368..447
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 448..520
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 570..635
FT /note="Peptidase C-terminal archaeal/bacterial"
FT /evidence="ECO:0000259|Pfam:PF04151"
FT DOMAIN 679..747
FT /note="Peptidase C-terminal archaeal/bacterial"
FT /evidence="ECO:0000259|Pfam:PF04151"
FT ACT_SITE 157
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 192
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 472
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 762 AA; 78951 MW; 13E22A46118F3ADD CRC64;
MTSKSLKICS IAAVALAVNT AIASDSEGLL KANLADNRAA VKSPLPKRYI VKYKEQSSFM
NFANTTSIES VTKDRLTQMG VRNAKFNPAI NANIAQLSDA QLKQLQNDPM VDYVEEDLPR
RLMAQTQPYG IAMVQADQVN DSVASAANNG KKICVIDSGL DLPHEDMGTN GGTVTGTNNS
GTGNWYQEGG PHGTHVAGTI AAIDNGVGVR GVIGSDPSLH IIKVFNASGW GYSSDLVSAM
NECKNAGSDV INMSLGGSGS STSERNGIQA IADAGVLLIA AAGNDGNPSN TTDIESFPAS
YDSVMSVAAI DSSKALADFS QKNSQVEIAA PGVDVYSTYP EGTGQVVSLS VGSSAYSVNA
MENTGSVTAP LYNFATGESI DSGANGKVCL IQRGNISFHD KVKNCQDSGG VGAVIYNNAA
GSFGGTLGDT NQTSIPAVTA TDADGATMLS QTGLSTTIDI GTGNYGMMSG TSMASPHVAG
VAALVWSHHP SCTAQEIRTA LNTTAEDLGA AGRDVKFGYG LVQAKDAIDH LQANGCSGDG
GTTPPTPGDN VLINGQTVSG IAANTNEEVL YTFEVPAGAT DVKVVMSGGS GDADLYTQFN
AQPTDSNYEC RPYANGNNET CNLTQSGGTY YVRVKAYSSF ANVSLTASYT EGNDGGGNGE
ITPIDDTVNN ISVSRRSWQR YTLDLAAGYS DLNITMSGGS GDADMYVTFG SQSTTSSYDC
RPYETGNNEN CSFSAPQAGT WYIDIYGYRA ASGVTLNVKA NP
//
