ID G0CAF7_XANCA Unreviewed; 438 AA.
AC G0CAF7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Serine protease {ECO:0000313|EMBL:AEL06792.1};
GN ORFNames=XCR_1899 {ECO:0000313|EMBL:AEL06792.1};
OS Xanthomonas campestris pv. raphani 756C.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=990315 {ECO:0000313|EMBL:AEL06792.1, ECO:0000313|Proteomes:UP000001633};
RN [1] {ECO:0000313|EMBL:AEL06792.1, ECO:0000313|Proteomes:UP000001633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=756C {ECO:0000313|EMBL:AEL06792.1,
RC ECO:0000313|Proteomes:UP000001633};
RX PubMed=21784931; DOI=10.1128/JB.05262-11;
RA Bogdanove A.J., Koebnik R., Lu H., Furutani A., Angiuoli S.V., Patil P.B.,
RA Van Sluys M.A., Ryan R.P., Meyer D.F., Han S.W., Aparna G., Rajaram M.,
RA Delcher A.L., Phillippy A.M., Puiu D., Schatz M.C., Shumway M.,
RA Sommer D.D., Trapnell C., Benahmed F., Dimitrov G., Madupu R., Radune D.,
RA Sullivan S., Jha G., Ishihara H., Lee S.W., Pandey A., Sharma V.,
RA Sriariyanun M., Szurek B., Vera-Cruz C.M., Dorman K.S., Ronald P.C.,
RA Verdier V., Dow J.M., Sonti R.V., Tsuge S., Brendel V.P., Rabinowicz P.D.,
RA Leach J.E., White F.F., Salzberg S.L.;
RT "Two new complete genome sequences offer insight into host and tissue
RT specificity of plant pathogenic Xanthomonas spp.";
RL J. Bacteriol. 193:5450-5464(2011).
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240}.
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DR EMBL; CP002789; AEL06792.1; -; Genomic_DNA.
DR RefSeq; WP_014507446.1; NC_017271.1.
DR AlphaFoldDB; G0CAF7; -.
DR KEGG; xcp:XCR_1899; -.
DR PATRIC; fig|990315.4.peg.1789; -.
DR HOGENOM; CLU_051649_0_0_6; -.
DR Proteomes; UP000001633; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07492; Peptidases_S8_8; 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; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034067; Serine_protease_KerA-like_dom.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
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.
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}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..438
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003397773"
FT DOMAIN 188..417
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 197
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 230
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 380
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 438 AA; 45228 MW; DF196603912AAB45 CRC64;
MTTPWAIGLL TALLSLTAPV CAQAADPQAI AAAAEAEKAD ADAKVPDSSR DILLAVANPL
TAPPARAGSS LIGYASSYYG AGQHAAARME ALKQRYQLRE VSAWPITSLG LYCAVLHPPA
GVSRDELIKA LSDDDGVELV QPVQEFSVFS TDASEKTGAL TGYNDPYVDL QRGFIATDAA
SAQAITQGRG VTVALVDTGV DISHPDLTSR IREVHDLVDD TPVTTSTDSH GTEVAGIIAA
GSNNHQGIVG MAPRAMLSIY KACWYAPSTG STARCNSFTL AKALAAINNS SARVVNLSLG
GPADPLLRKM LTHLVDHGRI VVAAMPPNGR LDGFPNDVPG VLVVRSSSAT AALPGVLSAP
GKDILTTQPN GRYDFTSGSS MATAHVSGMA ALLLSLSPSM DANALRALMQ RTSKVSDGQL
QVNAGAAVDA LALSKHSN
//
