PMRA_PECPM
ID PMRA_PECPM Reviewed; 222 AA.
AC Q70FH0; K4FN56;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Transcriptional regulatory protein PmrA;
GN Name=pmrA; OrderedLocusNames=W5S_4173;
OS Pectobacterium parmentieri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=1905730;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=SCC3193;
RX PubMed=14617142; DOI=10.1046/j.1365-2958.2003.03729.x;
RA Hyytiaeinen H., Sjoeblom S., Palomaeki T., Tuikkala A., Palva E.T.;
RT "The PmrA-PmrB two-component system responding to acidic pH and iron
RT controls virulence in the plant pathogen Erwinia carotovora ssp.
RT carotovora.";
RL Mol. Microbiol. 50:795-807(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCC3193;
RX PubMed=23045508; DOI=10.1128/jb.00681-12;
RA Koskinen J.P., Laine P., Niemi O., Nykyri J., Harjunpaa H., Auvinen P.,
RA Paulin L., Pirhonen M., Palva T., Holm L.;
RT "Genome sequence of Pectobacterium sp. strain SCC3193.";
RL J. Bacteriol. 194:6004-6004(2012).
CC -!- FUNCTION: Member of the two-component regulatory system PmrB/PmrA
CC involved in regulation of virulence. Unphosphorylated PmrA represses
CC extracellular enzyme genes. Phosphorylation of PmrA by PmrB relieves
CC such repression, which leads to activation of extracellular enzyme
CC genes. Phosphorylated PmrA seems to repress expression of the pmrCAB
CC operon. {ECO:0000269|PubMed:14617142}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- PTM: Phosphorylated by PmrB. {ECO:0000305}.
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DR EMBL; AJ583007; CAE47079.1; -; Genomic_DNA.
DR EMBL; CP003415; AFI92229.1; -; Genomic_DNA.
DR RefSeq; WP_014701628.1; NC_017845.1.
DR AlphaFoldDB; Q70FH0; -.
DR SMR; Q70FH0; -.
DR STRING; 1905730.W5S_4173; -.
DR EnsemblBacteria; AFI92229; AFI92229; W5S_4173.
DR KEGG; pec:W5S_4173; -.
DR PATRIC; fig|1166016.3.peg.4250; -.
DR eggNOG; COG0745; Bacteria.
DR HOGENOM; CLU_000445_30_1_6; -.
DR OrthoDB; 1020672at2; -.
DR Proteomes; UP000008044; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR CDD; cd00383; trans_reg_C; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR001867; OmpR/PhoB-type_DNA-bd.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR039420; WalR-like.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR48111; PTHR48111; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF00486; Trans_reg_C; 1.
DR SMART; SM00448; REC; 1.
DR SMART; SM00862; Trans_reg_C; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR PROSITE; PS51755; OMPR_PHOB; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW Cytoplasm; DNA-binding; Phosphoprotein; Repressor; Transcription;
KW Transcription regulation; Two-component regulatory system; Virulence.
FT CHAIN 1..222
FT /note="Transcriptional regulatory protein PmrA"
FT /id="PRO_0000232703"
FT DOMAIN 2..116
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DNA_BIND 124..218
FT /note="OmpR/PhoB-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01091"
FT MOD_RES 51
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 222 AA; 24868 MW; A27A6DB780A1099B CRC64;
MKLLIVEDDK LLQEGLLLAL SHEGYACDCA GTAKEADALI GSAHYSLVIL DLGLPDDDGL
ALLSRWRKNN YQHPVLILTA RDKVDDRVSG LDVGADDYLA KPFALTELQA RVRALIRRNQ
GSSNSKIQVD NITLDLNNQQ VLLDEKPVVL TPKEFAILSR LVLKAGYQVH RELLHQDIYA
WNDDPSSNSL EVHIHNLRQK IGKDRIRTLR GFGYLLTKGE QP