EXPR_XANCP
ID EXPR_XANCP Reviewed; 580 AA.
AC P23314;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Extracellular protease;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN OrderedLocusNames=XCC0851;
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS 528 / LMG 568 / P 25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190485;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2187155; DOI=10.1007/bf00391750;
RA Liu Y.-N., Tang J.-L., Clarke B.R., Dow J.M., Daniels M.J.;
RT "A multipurpose broad host range cloning vector and its use to characterise
RT an extracellular protease gene of Xanthomonas campestris pathovar
RT campestris.";
RL Mol. Gen. Genet. 220:433-440(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; X51635; CAA35962.1; -; Genomic_DNA.
DR EMBL; AE008922; AAM40166.1; -; Genomic_DNA.
DR PIR; S11890; S11890.
DR RefSeq; NP_636242.1; NC_003902.1.
DR RefSeq; WP_011036087.1; NC_003902.1.
DR AlphaFoldDB; P23314; -.
DR SMR; P23314; -.
DR STRING; 340.xcc-b100_3498; -.
DR MEROPS; S08.110; -.
DR EnsemblBacteria; AAM40166; AAM40166; XCC0851.
DR KEGG; xcc:XCC0851; -.
DR PATRIC; fig|190485.4.peg.926; -.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_011263_8_2_6; -.
DR OMA; WSADQGA; -.
DR Proteomes; UP000001010; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07496; Peptidases_S8_13; 1.
DR Gene3D; 3.40.50.200; -; 1.
DR InterPro; IPR007280; Peptidase_C_arc/bac.
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; IPR034176; Peptidases_S8_13.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF04151; PPC; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; SSF52743; 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 Disulfide bond; Hydrolase; Protease; Reference proteome; Secreted;
KW Serine protease; Signal; Zymogen.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT PROPEP 33..?136
FT /evidence="ECO:0000255"
FT /id="PRO_0000027018"
FT CHAIN ?137..580
FT /note="Extracellular protease"
FT /id="PRO_0000027019"
FT DOMAIN 147..465
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 177
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 237
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 409
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DISULFID 225..273
FT /evidence="ECO:0000250"
FT DISULFID 315..352
FT /evidence="ECO:0000250"
FT DISULFID 450..454
FT /evidence="ECO:0000255"
SQ SEQUENCE 580 AA; 57229 MW; 8C9A2CAE4E7F47CB CRC64;
MSTASLRKRT GSLTILGASA LTSLLLAMPA FAGEVYLDGL ATAQTHQKFI VTYKDGSTAL
ASPSALTTSL RTAARAVPAK AGKALGLNSV RRLALGPELV RADRALDRAE AETLMRQLAA
DPNVQSVEVD QILHATLTPN DTRLSEQWAF GTTNAGLNIR PAWDKATGSG TVVAVIDTGI
TSHADLNANI LAGYDFISDA TTARDGNGRD SNAADEGDWY AANECGAGIP AASSSWHGTH
VAGTVAAVTN NTTGVAGTAY GAKVVPVRVL GKCGGSLSDI ADAIVWASGG TVSGIPANAN
PAEVINMSLG GGGSCSTTMQ NAINGAVSRG TTVVVAAGND ASNVSGSLPA NCANVIAVAA
TTSAGAKASY SNFGTGIDVS APGSSILSTL NSGTTTPGSA SYASYNGTSM ASPHVAGVVA
LVQSVAPTAL TPAAVETLLK NTARALPGAC SGGCGAGIVN ADAAVTAAIN GGSGGGGGGG
NTLTNGTPVT GLGAATGAEL NYTITVPAGS GTLTVTTSGG SGDADLYVRA GSAPTDSAYT
CRPYRSGNAE TCTITAPSGT YYVRLKAYST FSGVTLRASY
