ID E2FHS2_ACIBA Unreviewed; 444 AA.
AC E2FHS2;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=pmrB {ECO:0000313|EMBL:ADK46865.1};
OS Acinetobacter baumannii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=470 {ECO:0000313|EMBL:ADK46865.1};
RN [1] {ECO:0000313|EMBL:ADK46865.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 19606 {ECO:0000313|EMBL:ADK46865.1};
RX PubMed=21576434; DOI=10.1128/AAC.00079-11;
RA Beceiro A., Llobet E., Aranda J., Bengoechea J.A., Doumith M., Hornsey M.,
RA Dhanji H., Chart H., Bou G., Livermore D.M., Woodford N.;
RT "Phosphoethanolamine Modification of Lipid A in Colistin-Resistant Variants
RT of Acinetobacter baumannii Mediated by the pmrAB Two-Component Regulatory
RT System.";
RL Antimicrob. Agents Chemother. 55:3370-3379(2011).
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};
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DR EMBL; HM149345; ADK46865.1; -; Genomic_DNA.
DR AlphaFoldDB; E2FHS2; -.
DR SMR; E2FHS2; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
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; 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; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 1.
DR PANTHER; PTHR45436:SF14; SENSOR PROTEIN QSEC; 1.
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; 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; PS50109; HIS_KIN; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 146..164
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 225..437
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 444 AA; 50699 MW; 6ADA7D662971E445 CRC64;
MHYSLKKRLI WGTSIFSVIL GCILIFSAYK VALQEVDEIL DTQMKYLAER TAEHPLKTVS
SKFDFHKTYH EEDLFIDIWA YKDQAHLSHH LHLLVPPVEQ AGFYSHKTAQ GIVRTYVLPL
KDYQIQVSQQ ERVREAFAWE LAGSMFIPYL IILPFAIFAL AAIIRRGLKP IDDFKNELKE
RDSEELTPIE VHDYPQELLP TIDEMNRLFE RISKAQNEQK QFIADAVHEL RTPVTALNLQ
TKILLSQFPE HESLQNLSKG LARIQHLVTQ LLALAKQDVT LSMVEPTGYF QLNDVALNCV
EQLVNLAMQK EIDLGFVRNE PIEMHSIEPT VHSIIFNLID NAIKYTPHQG VINISVYTDP
DHYACIQIED SGAGIDPENY DKVLKRFYRV HHHLEVGSGL GLSIVDRATQ RLGGTLTLDK
SLELGGLSVL VKLPKVLHLN ETRA
//
