ID A3U4E4_CROAH Unreviewed; 408 AA.
AC A3U4E4;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Extracellular alkaline serine protease {ECO:0000313|EMBL:EAP87111.1};
GN OrderedLocusNames=CA2559_00110 {ECO:0000313|EMBL:EAP87111.1};
OS Croceibacter atlanticus (strain ATCC BAA-628 / HTCC2559 / KCTC 12090).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Croceibacter.
OX NCBI_TaxID=216432 {ECO:0000313|EMBL:EAP87111.1, ECO:0000313|Proteomes:UP000002297};
RN [1] {ECO:0000313|EMBL:EAP87111.1, ECO:0000313|Proteomes:UP000002297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-628 / HTCC2559 / KCTC 12090
RC {ECO:0000313|Proteomes:UP000002297};
RX PubMed=20639333; DOI=10.1128/JB.00733-10;
RA Oh H.M., Kang I., Ferriera S., Giovannoni S.J., Cho J.C.;
RT "The complete genome sequence of Croceibacter atlanticus HTCC2559T.";
RL J. Bacteriol. 192:4796-4797(2010).
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; CP002046; EAP87111.1; -; Genomic_DNA.
DR RefSeq; WP_013185793.1; NC_014230.1.
DR AlphaFoldDB; A3U4E4; -.
DR STRING; 216432.CA2559_00110; -.
DR KEGG; cat:CA2559_00110; -.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_011263_1_7_10; -.
DR OrthoDB; 9798386at2; -.
DR Proteomes; UP000002297; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; 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 PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 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}; Reference proteome {ECO:0000313|Proteomes:UP000002297};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..408
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002660390"
FT DOMAIN 55..139
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 176..383
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 178
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 211
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 373
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 408 AA; 42170 MW; E6124E5A5B6A10E1 CRC64;
MKIFKPNTTF IAIAGMAVSS LFLSCEAEEQ ITETQNLKND SSVLQESQSQ AISGQYIVTL
NEAASRSIKN DDSYKGRLAN VNAFVNEMIA APHMKSTSVK QVYGFAMTGF TATLSPEQLK
SLQSDSRVAS VEPDVMVKLS VAKEETTAMT FVAQNTPYGI TRVNGGVDGT GKTAWIIDSG
IDLDHPDLNV DVDRSRSFVP GEPSPDDQNG HGSHVAGTVA AIDNGIGVIG VAPNAKVVAL
KVLGADGSGA TSGIIAALDY VAAVGEPGDA ANMSLGPAVP ILGINSALDN ATTRVGAKGI
GVAIAAGNST SIANLYSPAR ASGENVYTVS AMDSNDQFAY FSNFGSVVDY CAPGVSVYST
SMQGGYATLS GTSMAAPHVC GLLLLGDLRT DGNVFLDPDF NPDPIAVH
//
