UniProt: A0A0A7EL95

Database: UniProt
Entry: A0A0A7EL95_9GAMM

LinkDB:  A0A0A7EL95_9GAMM 
Original site:  A0A0A7EL95_9GAMM

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Ontology (2)   
   GO (2)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (15)   
   InterPro (9)   
   Pfam (2)   
   PROSITE (4)   
All databases (20)   

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ID   A0A0A7EL95_9GAMM        Unreviewed;       618 AA.
AC   A0A0A7EL95;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Alkaline serine protease {ECO:0000313|EMBL:AIY66717.1};
GN   ORFNames=OM33_16450 {ECO:0000313|EMBL:AIY66717.1};
OS   Pseudoalteromonas piratica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=1348114 {ECO:0000313|EMBL:AIY66717.1, ECO:0000313|Proteomes:UP000030341};
RN   [1] {ECO:0000313|EMBL:AIY66717.1, ECO:0000313|Proteomes:UP000030341}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OCN003 {ECO:0000313|EMBL:AIY66717.1,
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   -!- 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; AIY66717.1; -; Genomic_DNA.
DR   RefSeq; WP_040135171.1; NZ_CP009889.1.
DR   AlphaFoldDB; A0A0A7EL95; -.
DR   STRING; 1348114.OM33_16450; -.
DR   KEGG; pseo:OM33_16450; -.
DR   eggNOG; COG1404; Bacteria.
DR   HOGENOM; CLU_011263_1_7_6; -.
DR   OrthoDB; 9790784at2; -.
DR   Proteomes; UP000030341; Chromosome 2.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR   Gene3D; 2.60.120.380; -; 2.
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; IPR034193; PCSK9_ProteinaseK-like.
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; IPR037045; S8pro/Inhibitor_I9_sf.
DR   PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   Pfam; PF04151; PPC; 2.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF89260; Collagen-binding domain; 1.
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};
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..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..618
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002039234"
FT   DOMAIN          152..379
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          431..497
FT                   /note="Peptidase C-terminal archaeal/bacterial"
FT                   /evidence="ECO:0000259|Pfam:PF04151"
FT   DOMAIN          538..603
FT                   /note="Peptidase C-terminal archaeal/bacterial"
FT                   /evidence="ECO:0000259|Pfam:PF04151"
FT   ACT_SITE        161
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        194
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        346
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   618 AA;  64454 MW;  6C0306D14616119C CRC64;
     MFKYSKTMLL IASVCSANFA YADSEKLIQV NASKQIPNKY IVVFKTVPTS FANVGIAEQT
     SQNVDKVLGK YGIKANKVFG NTLNGAQYTL SKGQLKQLLK EDLVQFIEPE QIISIDPQVA
     TNANQSNAIW GLDRIDQRDL PLDSNYQYNF DGSGVTAYVI DTGVRNTHNE FGNRATSGWD
     FVDNDSDASD CNGHGTHVAG TIGGQQYGVA KNVNIVGVRV LGCNGSGSTS GVIDGINWVK
     NNASGPSVAN MSLGGGASTA IDQAVEAAVA SGVSFVVAAG NDNSNACNYS PARATTAITV
     GSTTSSDSRS SFSNYGTCLD IYAPGSSIKS AWYNSDSSEN TISGTSMAAP HVAGVVALYL
     DENSSLTPAQ IDSKLSAGAS KNKVSDAKSG SPNELLFALE GTVDPEPPTV TELIKDQAVS
     ASGAASSETN YFVDVPAGQS SLSISLSGGQ GDADLYVKQG SAPTTGSYDC RPYKNGNNES
     CEFNTPAAGK YYVMLQGYSA YSGASLVATY SADSGCTDCL DNGVPQTDLS GAANSQVFFK
     IDVPANQTLT VSTANGSGDV DLYVKKGSQP TTSDYECRPY RWGNNESCSL SSGATGGTYH
     ILLNAYSAYS GVTLTASY
//

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