ID A3QF26_SHELP Unreviewed; 605 AA.
AC A3QF26;
DT 17-APR-2007, integrated into UniProtKB/TrEMBL.
DT 17-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE SubName: Full=Peptidase S8 and S53, subtilisin, kexin, sedolisin {ECO:0000313|EMBL:ABO24074.1};
DE Flags: Precursor;
GN OrderedLocusNames=Shew_2208 {ECO:0000313|EMBL:ABO24074.1};
OS Shewanella loihica (strain ATCC BAA-1088 / PV-4).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=323850 {ECO:0000313|EMBL:ABO24074.1, ECO:0000313|Proteomes:UP000001558};
RN [1] {ECO:0000313|EMBL:ABO24074.1, ECO:0000313|Proteomes:UP000001558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1088 / PV-4 {ECO:0000313|Proteomes:UP000001558};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Serres G.,
RA Fredrickson J., Tiedje J., Richardson P.;
RT "Complete sequence of Shewanella loihica PV-4.";
RL Submitted (MAR-2007) 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; CP000606; ABO24074.1; -; Genomic_DNA.
DR RefSeq; WP_011866006.1; NC_009092.1.
DR AlphaFoldDB; A3QF26; -.
DR STRING; 323850.Shew_2208; -.
DR KEGG; slo:Shew_2208; -.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_011263_15_3_6; -.
DR OrthoDB; 9790784at2; -.
DR Proteomes; UP000001558; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07477; Peptidases_S8_Subtilisin_subset; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
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; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034202; Subtilisin_Carlsberg-like.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF00082; Peptidase_S8; 2.
DR PRINTS; PR00723; SUBTILISIN.
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:UP000001558};
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..605
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002658017"
FT DOMAIN 125..316
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 367..428
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 429..502
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 134
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 167
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 454
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 605 AA; 62607 MW; F852F571548FDDCC CRC64;
MKISKLAGMI SLITLGIAAS SQAADNRYVV QVDNQHKGIV KALAVKSGAT IELDGDGFFA
ASFNAQDLAQ VKGLLNNPHV KLVEEDQRRT LQSLYQDDAG DPMLSQLTPY AIYQSQADQV
DFVPGAGIKV CVIDSGLDRS NPDFNWGAIT GDNDSGTGDW DVNGGPHGTH VAGTIGAADN
GIGVVGMAPG VDMHIIKVFT ASGWAYSSDL AHATDLCSQA GANIISMSLG GGGASSIESN
AFEAFTQAGG LVVAAAGNDG NNARSYPAAY PAVMMVGAND ADNNIASFSQ FPSCSSGRGK
HATQDEMTCV EVTAGGVQTL STYPAEMATI AAMSADDVFF EASAMENIGS ASGSTYFMGT
AETLDTRAQG SVCVIDRGNI SFHDKVANCE ASGGIGAIIV NNVDGMLYGT LGDANSTQIP
AVGAALSDRT ALISATQASV SIASGDYGYM SGTSMATPAV SGVAALVWSN FPECTGSEIR
QALKATAEDQ GIPGHDEYFG YGIVKAKAAY DYLQSSGCNG QGGTPGTFSL NAEYEYARGK
HRVNLTTVAA SSPKVDIYRN EQLIATVAAN TLYTDSFGRK ATGNFNYKAC EENTQICTET
QSVNF
//
