ID Q2IXI2_RHOP2 Unreviewed; 456 AA.
AC Q2IXI2;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE RecName: Full=Signal transduction histidine-protein kinase/phosphatase MprB {ECO:0000256|ARBA:ARBA00040454};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
DE AltName: Full=Mycobacterial persistence regulator B {ECO:0000256|ARBA:ARBA00041776};
GN OrderedLocusNames=RPB_2373 {ECO:0000313|EMBL:ABD07078.1};
OS Rhodopseudomonas palustris (strain HaA2).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=316058 {ECO:0000313|EMBL:ABD07078.1, ECO:0000313|Proteomes:UP000008809};
RN [1] {ECO:0000313|EMBL:ABD07078.1, ECO:0000313|Proteomes:UP000008809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HaA2 {ECO:0000313|EMBL:ABD07078.1,
RC ECO:0000313|Proteomes:UP000008809};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Pelletier D.A.,
RA Kyrpides N., Anderson I., Oda Y., Harwood C.S., Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris HaA2.";
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
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DR EMBL; CP000250; ABD07078.1; -; Genomic_DNA.
DR RefSeq; WP_011441263.1; NC_007778.1.
DR AlphaFoldDB; Q2IXI2; -.
DR STRING; 316058.RPB_2373; -.
DR KEGG; rpb:RPB_2373; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_89_27_5; -.
DR OrthoDB; 9804645at2; -.
DR Proteomes; UP000008809; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 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 PANTHER; PTHR44936; SENSOR PROTEIN CREC; 1.
DR PANTHER; PTHR44936:SF12; SENSOR PROTEIN CREC; 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; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ABD07078.1};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Stress response {ECO:0000256|ARBA:ARBA00023016};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 179..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 199..251
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 259..456
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 456 AA; 49629 MW; D2A502E4BEEB46A4 CRC64;
MSRRRPRSLL TQVALLSFAA LLVAQFVSFW LFTADHAKRI RVAQRIEVVE RVAAVAALLD
KAPATARDDL LEAASSRSTR FEVATAPTVD RPVDLLGSDC GQRDCADLGL PAGLRMQEDF
VSPRDGGRFS DPPPRFRDRL VKSNLAPVAF KLSLPLRDAQ WLNVTSRFER PAIQLPPQVM
GTTLVSLALV LAALWFALRR VTRPLDQLAS AADGFGLDAP PPRMPTGGPR EVRALSDALA
RMHERLARML GERTRMLAAL GHDLRSPITA LRVRAEMVDD AENKERMIAT LDEMQQMVEA
TLAFARGVST DQPTEPVDLA ALASELAAEL SAIGPPIRIT SATPIVLPLR RVPLRRALRN
ILENAQRYGG GAEVRVEQDG TEVRMVIEDR GPGLPDSDLT RVFEPFVRLE TSRSRETGGT
GLGLPIARAI LQAHGATIAL ANRPEGGLRA TVTFAG
//
