PMRB_PSEAE
ID PMRB_PSEAE Reviewed; 477 AA.
AC Q9HV31;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Sensor protein kinase PmrB {ECO:0000303|PubMed:14507375};
DE EC=2.7.13.3 {ECO:0000250|UniProtKB:P40719};
GN Name=pmrB; OrderedLocusNames=PA4777;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP FUNCTION, AND INDUCTION BY CATIONIC ANTIMICROBIAL PEPTIDES.
RX PubMed=14507375; DOI=10.1046/j.1365-2958.2003.03673.x;
RA McPhee J.B., Lewenza S., Hancock R.E.;
RT "Cationic antimicrobial peptides activate a two-component regulatory
RT system, PmrA-PmrB, that regulates resistance to polymyxin B and cationic
RT antimicrobial peptides in Pseudomonas aeruginosa.";
RL Mol. Microbiol. 50:205-217(2003).
CC -!- FUNCTION: Member of the two-component regulatory system PmrA/PmrB that
CC plays a role in the regulation of resistance towards polymyxin B and
CC cationic antimicrobial peptides in response to limiting concentrations
CC of Mg(2+). Autoregulates also its own pmrAB operon under Mg(2+)-
CC limiting conditions (PubMed:14507375). May function as a membrane-
CC associated protein kinase that phosphorylates PmrA in response to
CC environmental signals leading to activation of specific gene promoters
CC (Probable). {ECO:0000269|PubMed:14507375, ECO:0000305|PubMed:14507375}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000250|UniProtKB:P40719};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: By cationic antimicrobial peptides and by Mg(2+)-limiting
CC conditions. {ECO:0000269|PubMed:14507375}.
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DR EMBL; AE004091; AAG08163.1; -; Genomic_DNA.
DR PIR; G83048; G83048.
DR RefSeq; NP_253465.1; NC_002516.2.
DR RefSeq; WP_003112923.1; NZ_QZGE01000018.1.
DR AlphaFoldDB; Q9HV31; -.
DR SMR; Q9HV31; -.
DR STRING; 287.DR97_2121; -.
DR PaxDb; Q9HV31; -.
DR PRIDE; Q9HV31; -.
DR EnsemblBacteria; AAG08163; AAG08163; PA4777.
DR GeneID; 881841; -.
DR KEGG; pae:PA4777; -.
DR PATRIC; fig|208964.12.peg.5004; -.
DR PseudoCAP; PA4777; -.
DR HOGENOM; CLU_000445_89_37_6; -.
DR InParanoid; Q9HV31; -.
DR OMA; IRIAMRP; -.
DR PhylomeDB; Q9HV31; -.
DR BioCyc; PAER208964:G1FZ6-4890-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IDA:PseudoCAP.
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; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
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 2: Evidence at transcript level;
KW ATP-binding; Kinase; Membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW Two-component regulatory system.
FT CHAIN 1..477
FT /note="Sensor protein kinase PmrB"
FT /id="PRO_0000449422"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 186..238
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 246..459
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT REGION 455..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 249
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ SEQUENCE 477 AA; 52706 MW; 687FFF838D1E2087 CRC64;
MSRAAVPSVR RRLLVNLLVG FVLCWLSVAA LTYHLSLKQV NRLFDDDMVD FGEAALRLLD
LATEDQAGED GSITEIIERS REAIQGLPLL RRESALGYAL WRDGQPLLSS LNLPPEITAQ
GPGFSTVEAQ GTHWRVLQLN IDGFQIWISE NLIYRQHTMN LLLFYSLFPL LLALPLLGGL
VWFGVARGLA PLREVQAEVQ QRSARHLQPI AVEAVPLEIR GLIDELNLLL ERLRTALEAE
RRLTSDAAHE IRTPLASLRT HAQVALRSED PKAHARGLLQ VSRSVERIST LMEQILLLAR
LDGDALLEQF HPVNLATLAE DVLSELARQA IDKDIELSLH QETVYVMGID LWLKAMVGNL
VGNALRYTPA GGQVEIRVEN RAQHAVLRVR DNGPGVALEE QQAIFTRFYR SPATSSGEGS
GLGLPIVKRI VELHFGSIGL GKGLEGKGLE VQVFLPKTQP DATRPPARGP DSGRSHI