ID B1KLL5_SHEWM Unreviewed; 807 AA.
AC B1KLL5;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=Peptidase S8 and S53 subtilisin kexin sedolisin {ECO:0000313|EMBL:ACA87312.1};
DE Flags: Precursor;
GN OrderedLocusNames=Swoo_3041 {ECO:0000313|EMBL:ACA87312.1};
OS Shewanella woodyi (strain ATCC 51908 / MS32).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=392500 {ECO:0000313|EMBL:ACA87312.1, ECO:0000313|Proteomes:UP000002168};
RN [1] {ECO:0000313|EMBL:ACA87312.1, ECO:0000313|Proteomes:UP000002168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51908 / MS32 {ECO:0000313|Proteomes:UP000002168};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Lykidis A., Zhao J.-S., Richardson P.;
RT "Complete sequence of Shewanella woodyi ATCC 51908.";
RL Submitted (FEB-2008) 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}.
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DR EMBL; CP000961; ACA87312.1; -; Genomic_DNA.
DR RefSeq; WP_012325648.1; NC_010506.1.
DR AlphaFoldDB; B1KLL5; -.
DR STRING; 392500.Swoo_3041; -.
DR KEGG; swd:Swoo_3041; -.
DR eggNOG; COG1404; Bacteria.
DR eggNOG; COG4935; Bacteria.
DR HOGENOM; CLU_011263_15_3_6; -.
DR Proteomes; UP000002168; Chromosome.
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; -; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 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; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR002884; P_dom.
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; 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; PF01483; P_proprotein; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF00082; Peptidase_S8; 2.
DR Pfam; PF04151; PPC; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF89260; Collagen-binding domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51829; P_HOMO_B; 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}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000002168};
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..807
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002764639"
FT DOMAIN 688..807
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
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 202
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 505
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 807 AA; 83869 MW; 0417439C111A8300 CRC64;
MTSTKPKTVA LSLSALAMAI SASVSAAPAF TPGVQSLNSG IEQASPLPKR YIVKFRNSNA
AASFQSQSNE MNEALYEPRS NEVFSHHRAM NSVSAKEMKR IGRSNSYTAK LNSKGIQSLR
LRPDVEYVEE DVPRRLLSET TPWGQTYVGA TSLSDSQAGN RTICIIDSGY DRDHSDLSGN
NVTGTNNSGT GNWYDPGNNN AHGTHVAGTI AAIANNSGVV GVMPNQNANI HVIKVFNESG
WGYSSSLVSA IDTCVNNGAN VVTMSLGGSS SSTTERNALN AHESNGVLLI AAAGNDGDNT
HSYPASYDAV MSVAAVDSNK DHAAFSQYTN QVEISGPGEA ILSTVTAGEG RLADITVGGQ
SYFDQGVVPH NRYVKSGTNH VPTPVIGNVT AELAECTVSG TTFNCGNMSN RICLVERIGN
QGATYPEIDA VKACNSAGAS GVIVYSNTDL PGLQNPFLVD TNNEAALVSV SVDRATGQAL
QGQIGSTVTV ANTDNEDYEY YNGTSMATPH VSGVATLVWS HHTQCSAAQI RAALHATAED
LDAAGRDDKT GYGLVDAVAA KAYLDESCDG PTDPGTGPGD NVLVNGTAKT SLAGAKDAEL
HYSIDVPAGA TDLSFTMSGG TGDADLYVQY GAAPTTGSYD CRPWKSGNSE SCPISNVQTG
TYYVMVQGYS AFSGVSLVAN YTESNGGGNP GGGAASYTNN TTYAIPDNRS AGISSAISAT
RTGDSGSVSV AVDISHTYIG DLQVELHSPS GQVAILHDNT GGSANDINKT YTVDMSGVES
AGQWTLKAVD SARRDTGTIN SWTLSFQ
//
