ID Q2VZM5_MAGSA Unreviewed; 1258 AA.
AC Q2VZM5;
DT 10-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 10-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 137.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=amb4146 {ECO:0000313|EMBL:BAE52950.1};
OS Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Magnetospirillaceae; Paramagnetospirillum.
OX NCBI_TaxID=342108 {ECO:0000313|EMBL:BAE52950.1, ECO:0000313|Proteomes:UP000007058};
RN [1] {ECO:0000313|EMBL:BAE52950.1, ECO:0000313|Proteomes:UP000007058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AMB-1 / ATCC 700264 {ECO:0000313|Proteomes:UP000007058};
RX PubMed=16303747; DOI=10.1093/dnares/dsi002;
RA Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.;
RT "Complete genome sequence of the facultative anaerobic magnetotactic
RT bacterium Magnetospirillum sp. strain AMB-1.";
RL DNA Res. 12:157-166(2005).
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 -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP007255; BAE52950.1; -; Genomic_DNA.
DR RefSeq; WP_011386495.1; NC_007626.1.
DR AlphaFoldDB; Q2VZM5; -.
DR STRING; 342108.amb4146; -.
DR KEGG; mag:amb4146; -.
DR HOGENOM; CLU_004332_0_0_5; -.
DR OrthoDB; 9801651at2; -.
DR Proteomes; UP000007058; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00088; HPT; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 1.10.8.500; HAMP domain in histidine kinase; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR024478; HlyB_4HB_MCP.
DR InterPro; IPR036641; HPT_dom_sf.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF12729; 4HB_MCP_1; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 1.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:BAE52950.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000007058};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 198..219
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 217..270
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 471..528
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 550..601
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 619..840
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 857..977
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1006..1121
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1158..1255
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 447..474
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 910
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1055
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1197
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1258 AA; 136138 MW; 9FD400E8E7FDC9F5 CRC64;
MTFLLNALER LRLTTKLVLG FSVFLLMIVG LGLYSLLVQR GLNDEIQTLY TRELVGISSL
KDGRIELAKM GRALRQAILA REPAERDRAL RQLSQAEAAL HTEMSHVRPT LVREENRRNL
ARFDDGFKDF KANVDQAVAL LRTNPADAAV FVATPAFQLV AAASDEALEA VVRVKERGAQ
ESARLAQEGY ERGQRLTLLL LLGGGGMGLL FAVLIGMSIR RPATRVRDVV EKLVGGQLDQ
AVPHTDYPNE IGALARSIDV LRGEALQMES QRWVKTHLAN LSAELQAATT MAGLAQTFLS
VMAPLLKVGH GVFYIHEEEA GRLRLLGGYA FRQRKTLDQT FAMGEGLIGQ CALERSPFII
TRPPSDYVRI DCGMAEMVPK TIAVLPVLRG ERLLAVVELA TLEAFGPAEQ SLLDGALPVL
AMSLEILERG AKTAALLEET RVQAATLAAS ERQVAARKEE LEAINGQLAE AEERSRLILG
SVDEGICGLA QDGTMSFVNP AGARMLGYGL DEIVGKPLHA LAHHTYPDGT PFPRECCSMF
LTSQDGQPRT EVDEVLWRKD GTSFPVEYST TPVLKDGTVV GTVVTFRDIT ERKRADALLH
QALDRAEAAS QAKADFLANM SHEIRTPMNA IIGMSHLALK TELNPRQRDY VRKIQQSGQH
LLGIINDILD FSKIEAGKLS VEKTAVHLDT VLDNVANLIS EKTIAKGLEL IFDVASDVPN
DMVGDPLRLG QILINYANNA VKFTETGEIV VAVRLAEDLG EAVRLRFEVR DTGIGLSAEQ
MGRLFQSFQQ ADTSTTRKYG GTGLGLAISR KLAELMDGEV GVESQPGRGS TFWFTACLGK
GRPRRALVPK PDLRGRHMLV VDDNENARAV LVDMLTSMSF RVEAVESGAA AVARVREVAG
AKPFEVVFLD WQMPGMDGIE TARAILGLGL TSPPHMIMVT AHGREEVMKA AESAGIEDVL
IKPVNPSIMF DAVMRALGAA LEGDPEEAAA GREVSDDALA SLRGLRVLLA EDNDFNQQVA
TELLADGGVE VEVAENGKIA VDMVMAAPYD MVLMDMQMPV MDGVAATREI RRLGFGDLPV
IAMTANAMQA DRDRCAAAGM NDYLTKPIDP DELFACLLKW RGVAPTAVVA PAAPAGAVPL
LPEIDPDVFD FERMGPIYKW DMARLRPILA AFLDDAGTKV ARLEAETDLA ALREVAHGLK
GTANTAGALR LGRLAADVEN SARDGNDAAA GMLIPLLPPT LSELRDALAP VLDDRGVP
//
