ID   PMRB_PECPM              Reviewed;         364 AA.
AC   Q70FG9; K4FYI2;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Sensor histidine kinase PmrB;
DE            EC=2.7.13.3;
GN   Name=pmrB; OrderedLocusNames=W5S_4174;
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. Functions probably as a sensor
CC       protein kinase which is autophosphorylated at a histidine residue and
CC       transfers its phosphate group to PmrA in response to external pH and
CC       iron. {ECO:0000269|PubMed:14617142}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000305}.
CC   -!- PTM: Autophosphorylated. {ECO:0000305}.
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DR   EMBL; AJ583007; CAE47080.1; -; Genomic_DNA.
DR   EMBL; CP003415; AFI92230.1; -; Genomic_DNA.
DR   RefSeq; WP_014701629.1; NC_017845.1.
DR   AlphaFoldDB; Q70FG9; -.
DR   SMR; Q70FG9; -.
DR   STRING; 1905730.W5S_4174; -.
DR   EnsemblBacteria; AFI92230; AFI92230; W5S_4174.
DR   KEGG; pec:W5S_4174; -.
DR   PATRIC; fig|1166016.3.peg.4251; -.
DR   eggNOG; COG0642; Bacteria.
DR   HOGENOM; CLU_000445_89_37_6; -.
DR   OrthoDB; 692375at2; -.
DR   Proteomes; UP000008044; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Kinase; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Transferase; Transmembrane;
KW   Transmembrane helix; Two-component regulatory system; Virulence.
FT   CHAIN           1..364
FT                   /note="Sensor histidine kinase PmrB"
FT                   /id="PRO_0000232702"
FT   TOPO_DOM        1..14
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        15..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        36..65
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        66..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        87..364
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          90..142
FT                   /note="HAMP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT   DOMAIN          150..358
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         153
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   364 AA;  41089 MW;  571356AF6907E48F CRC64;
     MKGDSEAVTS MRRRLVLALG GILLVCQMIS VFWLWHESEE QIGLLVDKSL SAAAQNMQID
     QEINEAIASL SIPSLVMVIL TLLMCFQAVS WITRPLSRLQ EELQDRTAEN LEPLPQQSDI
     KEIAAVTHTI NQLFQRLDET LKRDRQFTAD VAHELRTPLA GIRLHLELHQ QQHQIDCSSL
     IKRIDKMVKT VEQLLLLARV GQEFSAGHHE NVAFLKDVIF PMQDELAEML QKRQQRLKWV
     LPQEDVTLHG DATLLQLLLR NLVENAYRYS PETSQITVSL NTQQHVELQI EDEGQGIDES
     KVGELSKAFV RMDSRYGGIG LGLSIVTRIA QLHNGKFFLS NRPQGPGALA RVVLTTPDNY
     PDAA