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Database: UniProt
Entry: S0EXI3_CHTCT
LinkDB: S0EXI3_CHTCT
Original site: S0EXI3_CHTCT 
ID   S0EXI3_CHTCT            Unreviewed;      1049 AA.
AC   S0EXI3;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Subtilisin-like serine proteases {ECO:0000313|EMBL:CCW36403.1};
GN   ORFNames=CCALI_02610 {ECO:0000313|EMBL:CCW36403.1};
OS   Chthonomonas calidirosea (strain DSM 23976 / ICMP 18418 / T49).
OC   Bacteria; Armatimonadota; Chthonomonadetes; Chthonomonadales;
OC   Chthonomonadaceae; Chthonomonas.
OX   NCBI_TaxID=1303518 {ECO:0000313|EMBL:CCW36403.1, ECO:0000313|Proteomes:UP000014227};
RN   [1] {ECO:0000313|Proteomes:UP000014227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23976 / ICMP 18418 / T49
RC   {ECO:0000313|Proteomes:UP000014227};
RA   Lee K.C.Y., Morgan X.C., Dunfield P.F., Tamas I., Houghton K.M.,
RA   Vyssotski M., Ryan J.L.J., Lagutin K., McDonald I.R., Stott M.B.;
RT   "Genome sequence of Chthonomonas calidirosea, the first sequenced genome
RT   from the Armatimonadetes phylum (formally candidate division OP10).";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR   EMBL; HF951689; CCW36403.1; -; Genomic_DNA.
DR   RefSeq; WP_016483912.1; NC_021487.1.
DR   AlphaFoldDB; S0EXI3; -.
DR   STRING; 454171.CP488_01481; -.
DR   KEGG; ccz:CCALI_02610; -.
DR   PATRIC; fig|1303518.3.peg.2713; -.
DR   eggNOG; COG1404; Bacteria.
DR   HOGENOM; CLU_291137_0_0_0; -.
DR   InParanoid; S0EXI3; -.
DR   OrthoDB; 9798386at2; -.
DR   Proteomes; UP000014227; Chromosome.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.4070; -; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR025965; FlgD/Vpr_Ig-like.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   Pfam; PF13860; FlgD_ig; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 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:UP000014227};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..1049
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004485872"
FT   DOMAIN          153..419
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          961..1034
FT                   /note="FlgD/Vpr Ig-like"
FT                   /evidence="ECO:0000259|Pfam:PF13860"
FT   ACT_SITE        157
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        196
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        369
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   1049 AA;  110499 MW;  28533EBE68F26CA9 CRC64;
     MVKKFGLLIP VLALLLLTSN AVRSRADGLP GAQAAFVDGQ VVLYCQPGTS QNDVNALAAK
     VNAQQVIPLL LKDCYELILP ASSATDAGTL NAVATLKGDP RVRWVGPNKI FHLMASPPTA
     TPNDPYYTNG DQWPLPQINM PAAWAIEKGT ANVADIDTGF DNTHPDLAGQ YILPGYNSVD
     GSTNNTPSGT DAANQHGVST SSIMVAITNN AIGMASICGW GTTKCLGIKA GDANGFTEAA
     LVNASQYVLN VAQQDNIVVV NESLGAPGDP TDTSDPYYQA TKALSDAGII VVVAAGNDSS
     DNHQTTPAGF TFPNLLTVSA LNRNSQLAFY SSFGKVDISA PGGEQTSATD PNGFLVAVNG
     SYGFEQGTSM AAPVVSGVIA LLRSIPAVTP TAAIQAIEQS ANHVITGQQQ VPDPKYGYGE
     VDAYQALLRV IGHVEVDSPI GIDNATGLST DPSGNPPPPV ETLKPTFTFG VRNIPLSNIN
     IVIMNPDGTT TPLVTNGTPA AGVTNFSVSG DTTSSYPVYS ISFRYAFNTV LASSQITVQI
     TGTPTNPNIP TPQQTVTFNL QPHRFPAGLS LISIPIYESA TDSPSGSFRN DIRQILSDPT
     AVLYSWGIQP TLNSAGQATA QGVYTPTPGT VGASASFTVS GIPASSTPAT NPPLGLGFFL
     KTTASDIYRT YGNYIASQFV NIPLHEGWNL VGDPFPFAVS FNICSFQTPG GNLYSAQQAA
     DAHLILPFIY RYVGGSYQFD TLPQGLLRPW EGSWIYVIPA NPNSLSTNYV LTLVVPPTGS
     ISDTLGRSTT ANTPSAGGPN NWRLQLVATS GSAVDGHNYI GVSAQQTDPS FTRAPKPPQL
     MNDISLSILE QGRGVQKEPY AMSLHAPAAT QTWQVLVQFA NKGTPVTVSW PNVAQIPHNI
     KLVLTDQTTG QQIDMRTRSA YQFMPAAQET ARQFQITAST VSTSGRALIT DLFVDPVNSN
     RAAGAAGFDI RYNISRDANV DIEILASNGR VIGRAQPSRA VTAGTNRAFW NGRDLAGNPV
     PTGVYMVQLR AVTASGDVTR QTVPLTITR
//
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