ID B0RUN7_XANCB Unreviewed; 438 AA.
AC B0RUN7;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Subtilase family serine protease, probable {ECO:0000313|EMBL:CAP51956.1};
GN ORFNames=XCCB100_2596 {ECO:0000313|EMBL:CAP51956.1};
OS Xanthomonas campestris pv. campestris (strain B100).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=509169 {ECO:0000313|EMBL:CAP51956.1, ECO:0000313|Proteomes:UP000001188};
RN [1] {ECO:0000313|EMBL:CAP51956.1, ECO:0000313|Proteomes:UP000001188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B100 {ECO:0000313|EMBL:CAP51956.1,
RC ECO:0000313|Proteomes:UP000001188};
RX PubMed=18304669; DOI=10.1016/j.jbiotec.2007.12.013;
RA Vorholter F.J., Schneiker S., Goesmann A., Krause L., Bekel T., Kaiser O.,
RA Linke B., Patschkowski T., Ruckert C., Schmid J., Sidhu V.K., Sieber V.,
RA Tauch A., Watt S.A., Weisshaar B., Becker A., Niehaus K., Puhler A.;
RT "The genome of Xanthomonas campestris pv. campestris B100 and its use for
RT the reconstruction of metabolic pathways involved in xanthan
RT biosynthesis.";
RL J. Biotechnol. 134:33-45(2008).
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240}.
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DR EMBL; AM920689; CAP51956.1; -; Genomic_DNA.
DR AlphaFoldDB; B0RUN7; -.
DR KEGG; xca:xcc-b100_2596; -.
DR HOGENOM; CLU_051649_0_0_6; -.
DR Proteomes; UP000001188; 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_5002752429"
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; 45184 MW; 4BAFAE7A4E1BB5A5 CRC64;
MTTPWAIGLL AALLSLTAPV CAQAADPQAI AAAAEAEKAD ADAKVPDSSR DILLAVANPL
TAPPARAGSS LIGYASSYYG AGQHAAARME ALKQRYQLRE VSAWPITSLG LYCAVLHPPA
GVSRDELIKA LSDDDGVELV QPVQEFSVFS TDASEKTGAL TGYNDPYVDL QRGFIATNAA
SAQAVTQGRG VTVAVVDTGV DTSHPDLKSR IREVHDLVDD TPVTTSTDSH GTEVAGIIAA
GSNNHQGIVG MAPRAMLSIY KACWYAPSTG STARCNSFTL AKALAAINNS SARVVNLSLG
GPADPLLRKM LTHLVDHGRI VVAAMPPNGR LDGFPNDVPG VLVVRSSSAT AALPGVLSAP
GKDILTTQPN GRYDFTSGSS MATAHVSGMA ALLLSLSPSM DANALRALMQ RTSKVSDGQL
QVNAGAAVDA LALSKHSN
//
