RFAY_XANCP
ID RFAY_XANCP Reviewed; 400 AA.
AC P46358;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Probable RNA polymerase sigma factor RfaY;
GN Name=rfaY; OrderedLocusNames=XCC1143;
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 [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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-207.
RX PubMed=7579621; DOI=10.1094/mpmi-8-0768;
RA Dow J.M., Osbourn A.E., Wilson T.J., Daniels M.J.;
RT "A locus determining pathogenicity of Xanthomonas campestris is involved in
RT lipopolysaccharide biosynthesis.";
RL Mol. Plant Microbe Interact. 8:768-777(1995).
CC -!- FUNCTION: Sigma factors are initiation factors that promote the
CC attachment of RNA polymerase to specific initiation sites and are then
CC released. This sigma factor is involved in lipopolysaccharide
CC biosynthesis and pathogenicity.
CC -!- SIMILARITY: Belongs to the sigma-70 factor family. ECF subfamily.
CC {ECO:0000305}.
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DR EMBL; AE008922; AAM40442.1; -; Genomic_DNA.
DR EMBL; U19896; AAA92044.1; -; Genomic_DNA.
DR RefSeq; NP_636518.1; NC_003902.1.
DR RefSeq; WP_011036343.1; NC_003902.1.
DR AlphaFoldDB; P46358; -.
DR SMR; P46358; -.
DR STRING; 340.xcc-b100_3196; -.
DR EnsemblBacteria; AAM40442; AAM40442; XCC1143.
DR KEGG; xcc:XCC1143; -.
DR PATRIC; fig|190485.4.peg.1222; -.
DR eggNOG; COG1595; Bacteria.
DR HOGENOM; CLU_679548_0_0_6; -.
DR OMA; RIVLACQ; -.
DR Proteomes; UP000001010; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016987; F:sigma factor activity; IEA:UniProtKB-KW.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro.
DR GO; GO:0006950; P:response to stress; IEA:UniProt.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR039425; RNA_pol_sigma-70-like.
DR InterPro; IPR014284; RNA_pol_sigma-70_dom.
DR InterPro; IPR000838; RNA_pol_sigma70_ECF_CS.
DR InterPro; IPR007627; RNA_pol_sigma70_r2.
DR InterPro; IPR013249; RNA_pol_sigma70_r4_t2.
DR InterPro; IPR013325; RNA_pol_sigma_r2.
DR InterPro; IPR013324; RNA_pol_sigma_r3/r4-like.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR43133; PTHR43133; 1.
DR Pfam; PF04542; Sigma70_r2; 1.
DR Pfam; PF08281; Sigma70_r4_2; 1.
DR SUPFAM; SSF88659; SSF88659; 1.
DR SUPFAM; SSF88946; SSF88946; 1.
DR TIGRFAMs; TIGR02937; sigma70-ECF; 1.
DR PROSITE; PS01063; SIGMA70_ECF; 1.
PE 3: Inferred from homology;
KW DNA-binding; Reference proteome; Sigma factor; Transcription;
KW Transcription regulation.
FT CHAIN 1..400
FT /note="Probable RNA polymerase sigma factor RfaY"
FT /id="PRO_0000094013"
FT DNA_BIND 165..184
FT /note="H-T-H motif"
FT /evidence="ECO:0000250"
FT MOTIF 62..75
FT /note="Polymerase core binding"
FT CONFLICT 1..6
FT /note="MHADTL -> MLVPGHGFRRCTPTPW (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 19
FT /note="A -> G (in Ref. 2; AAA92044)"
FT /evidence="ECO:0000305"
FT CONFLICT 23
FT /note="Q -> K (in Ref. 2; AAA92044)"
FT /evidence="ECO:0000305"
FT CONFLICT 31
FT /note="A -> V (in Ref. 2; AAA92044)"
FT /evidence="ECO:0000305"
FT CONFLICT 38
FT /note="A -> P (in Ref. 2; AAA92044)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="A -> V (in Ref. 2; AAA92044)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="H -> Y (in Ref. 2; AAA92044)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="Q -> E (in Ref. 2; AAA92044)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="S -> I (in Ref. 2; AAA92044)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="A -> P (in Ref. 2; AAA92044)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="A -> G (in Ref. 2; AAA92044)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="A -> V (in Ref. 2; AAA92044)"
FT /evidence="ECO:0000305"
FT CONFLICT 206..207
FT /note="TA -> DR (in Ref. 2; AAA92044)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 400 AA; 42322 MW; 4C19FFE15CE91FAE CRC64;
MHADTLDAML HHELPHAAAG CQQAYGRIVT ACQNTVTAIA LAITRDVAAS EDIAQEAFLR
AWQRLAQLHQ PASFLPWLRQ ITRNLARDWL RSHRHRPLSG EAADLAIAMA ADPSPSPAEQ
ALQVEEERAA LEIMSALPND SREILLLYYR EGQRSQQVAS LLGLSDAAVR KRLSRARATV
RNELLQRFDT FARGSAPGVA FATTVTAATM LAAPGTASAA IALGGIGSLG GVGKLGASGL
SGSALTSGSA AGALSVLLGM PMAIALLAIT GVTLTTYMSG AYLLRFATTA REAAAIRGFT
RLSTLTAALT CGAPLLLRAF GAPKWLALCV LAVGMSVVCY HTLGTLPRIM QPMLERDARR
RGTTRPPLLY RCMFSRSAIA VSLAAVIVPI AYRYGVLGLV
