ID A9KVN5_SHEB9 Unreviewed; 704 AA.
AC A9KVN5;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE SubName: Full=Peptidase S8 and S53 subtilisin kexin sedolisin {ECO:0000313|EMBL:ABX50134.1};
DE Flags: Precursor;
GN OrderedLocusNames=Sbal195_2968 {ECO:0000313|EMBL:ABX50134.1};
OS Shewanella baltica (strain OS195).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=399599 {ECO:0000313|EMBL:ABX50134.1, ECO:0000313|Proteomes:UP000000770};
RN [1] {ECO:0000313|EMBL:ABX50134.1, ECO:0000313|Proteomes:UP000000770}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS195 {ECO:0000313|EMBL:ABX50134.1,
RC ECO:0000313|Proteomes:UP000000770};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Brettar I.,
RA Rodrigues J., Konstantinidis K., Klappenbach J., Hofle M., Tiedje J.,
RA Richardson P.;
RT "Complete sequence of chromosome of Shewanella baltica OS195.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240, ECO:0000256|RuleBase:RU003355}.
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DR EMBL; CP000891; ABX50134.1; -; Genomic_DNA.
DR RefSeq; WP_006085524.1; NC_009997.1.
DR AlphaFoldDB; A9KVN5; -.
DR MEROPS; S08.125; -.
DR GeneID; 11773050; -.
DR KEGG; sbn:Sbal195_2968; -.
DR HOGENOM; CLU_019254_0_0_6; -.
DR Proteomes; UP000000770; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProt.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR034182; Kexin/furin.
DR InterPro; IPR002884; P_dom.
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 PANTHER; PTHR42884:SF32; EXTRACELLULAR SERINE PROTEASE; 1.
DR PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1.
DR Pfam; PF01483; P_proprotein; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51829; P_HOMO_B; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 547..701
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT ACT_SITE 173
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 211
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 447
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 704 AA; 74763 MW; 72AF078FD4AF2162 CRC64;
MRMSIVALSI TAALLAGCGS DKKAPEPVAK INTAPTTADM TIDVSQSLLF TGKLDATDAE
GGLTYSLVDP TDLKLGTLTL VNKSTGEFTY ASNASEGTDV VRFKVSDGQY QAEGTLTIHI
KNGDPLYAYQ WHLKNTGQNS FALNRGIAGE DMNVSEAISK QVMGQGITVA VVDDGLEISH
PDLVNNTVKG GSYNLITGSV DPTPFSGESG HGTAVGGIIA AEGWNGIGGR GVAPKAQLIG
FNFLDSDPTG KVTNVQTFEN FTKSHGASAY SDSARVFNQS YGYSVPFPHG FDEDESEVYR
DVATQSFDGK GSIFVKSAGN GYDYYRFSTF WLPGDYFSAT AENPANHGLP FHNSNMSSDN
ANVYNLVVSA INAKGVLSSY SSVGSNIFVT APGGEYGEVN PAIVTTDRVG CENGSAIAED
RPSTPFHGGL HPLNSNCDYT STMNGTSSAA PNTSGAVAVI MSANPDLTWR DVRNVLAKTS
TKVNADIAAK TVTIGEGDAA QEYVAIPEWQ ENAAGYSFHN FYGFGRVNVS EAVKLAKSYA
EDLGEYVVTE WQASQELAKA IPDADVNGVS DTQMVADDLI IEAVQIELTA DHLRLPDLAV
ELISPAGTKS VLMTPYNGLV YQGVMDKTDP EDLITGFDAT PMLSNAFYGE SAKGEWTIKL
IDVNSGSYKF IKYDQGYISI PNEADGKLKG WSIRFHGHAA KSAS
//
