ID Q2W5X4_MAGSA Unreviewed; 1959 AA. AC Q2W5X4; DT 10-JAN-2006, integrated into UniProtKB/TrEMBL. DT 10-JAN-2006, sequence version 1. DT 27-MAR-2024, entry version 123. DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438}; DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438}; GN OrderedLocusNames=amb1947 {ECO:0000313|EMBL:BAE50751.1}; OS Magnetospirillum magneticum (strain AMB-1 / ATCC 700264). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales; OC Magnetospirillaceae; Paramagnetospirillum. OX NCBI_TaxID=342108 {ECO:0000313|EMBL:BAE50751.1, ECO:0000313|Proteomes:UP000007058}; RN [1] {ECO:0000313|EMBL:BAE50751.1, 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 --------------------------------------------------------------------------- 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; BAE50751.1; -; Genomic_DNA. DR RefSeq; WP_011384350.1; NC_007626.1. DR STRING; 342108.amb1947; -. DR KEGG; mag:amb1947; -. DR HOGENOM; CLU_000445_34_2_5; -. DR OrthoDB; 9789238at2; -. DR Proteomes; UP000007058; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro. DR CDD; cd14014; STKc_PknB_like; 1. DR Gene3D; 3.30.450.40; -; 1. DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR041664; AAA_16. DR InterPro; IPR003018; GAF. DR InterPro; IPR029016; GAF-like_dom_sf. DR InterPro; IPR003594; HATPase_C. DR InterPro; IPR036890; HATPase_C_sf. DR InterPro; IPR005467; His_kinase_dom. DR InterPro; IPR036641; HPT_dom_sf. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR004358; Sig_transdc_His_kin-like_C. DR InterPro; IPR008266; Tyr_kinase_AS. DR PANTHER; PTHR43642; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE G; 1. DR PANTHER; PTHR43642:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE G; 1. DR Pfam; PF13191; AAA_16; 1. DR Pfam; PF01590; GAF; 1. DR Pfam; PF02518; HATPase_c; 1. DR Pfam; PF00069; Pkinase; 1. DR PRINTS; PR00344; BCTRLSENSOR. DR SMART; SM00065; GAF; 1. DR SMART; SM00387; HATPase_c; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1. DR SUPFAM; SSF55781; GAF domain-like; 1. DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS50109; HIS_KIN; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. PE 4: Predicted; KW Reference proteome {ECO:0000313|Proteomes:UP000007058}. FT DOMAIN 1..274 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT DOMAIN 1820..1952 FT /note="Histidine kinase" FT /evidence="ECO:0000259|PROSITE:PS50109" SQ SEQUENCE 1959 AA; 214912 MW; B61D30F808F78D33 CRC64; MSVPSEFKVA DILCRDEETL LARGTAAGGR AVLLRSTSSA RPSQPVIDRL RREFALRSEI DAAWGAVPLS LDEVSGRLTL TLSDPGGVPL SQVIASRSGP LRMADVARLL RLSALLARTL GRVHVKGLIH KDITPSNILI DEAGATVTFT GFGAASQLRR EQRHNQGAES VCGTFAYMAP EQTGRMNRSV DSRSDLYSLG VVLYEMFTGL RPFSAVDPME WVHCHIARQP SPPHDRVAGL PDQISAIIMK LLAKTAEERY QTAEGLASDL EACLAEWTTA GRISGFPLAG SDHSGILTIP EHLYGRERES DILLAAFRRV ADDGMPELVL VSGYSGVGKS ALVNQIHPAM VERDGMFGAG KFDQHKRDIP YSTFAQAFHT LIRQILGAPE SDIRRWREAF LDAVGPNGGL LIDLIPQLEL VVGEQPGVPE LPPGEAQVRF LTVFRRFVSV LARPEQPLVL FLDDLQWMDN GSMKLLEHLM THPEVRHLLL IGSYRDNEVD SSHPLMLSVE TIRKGGRPVD DIVLKPLNED DLGHLVADTL RCAGERAAPL VRLIHQKTAG NPFFAIQFLS TLAEEKLLWF DQSKAEWRWD LGRIGDMGFS DNVVILMAAK LRRLPEADQA ELRRIACLGN GTTLGTLAMA YDRTEEECLG SLEKAIQAGF LIRNGDRLSF THDRIQEAAY LSLPIAEMVA THLQIGRRML ESLSAEEVDD RLFDVIHHLN LGRQMITSQA ERDLLAGLNI QAGRKAKASS ANASARVYFT LARNLLGADC WDVAHDNTFA LFLDLSECEY LVGNHAQADA LFELLLGKAA TDDQSAQVWR LRFRMFMVSG RFGDAVAVAV KALERFGLAC PETEEDTASA VQAARQELAG LLKGRHVADL VRLPECHVPA VRALIGLIAD AIPAVYHVRP LLYPFLGLTA INLSLHHGVT EDSSAAFSGY SVSLVGRFED FRTGLEFSEL ALKLGERFDS APLKGTLLFR HGYFVTPWSK PIASIMPVLE ETFRTCLDTG NLIYAAYVAY ASAWMLFEKG EPLDVVLAHM RKYTPFAANA RIPFAILMLR LQELFIAGLQ GVELDVKPGI AGADSAENSY EALVATAHGY GIAFYHVVRQ VTPYLMGRYE EALGAARETA ALVPKISSSV IETSHHFYGA LAITALYPSA EPERREEMAP WLAEHHRKLA LWAEHCPETF AARAALIDAE MAALSGGGNE VMRLYERAIL TAREHGQLHC EAIANERAGQ FCLEQGLPSI AENYLRNARY CYTRWGALAK VAQLDQNFPR LAEAALADGA MTSFSGSADG LDLMTVIKAQ QAVSGEIVLG KLVESLLRIV VEHAGADRGL LILRHGDSFR IEAEAVVEGD LIAVSTCAAP PTSDDLPLTV FQYVARTRER VVIDNAIGPN TYMTEGYAAR SGVKSVMCLP VVTHGALSAV LYLENRLAAG AFTRKRVAVL DLLATQASIS LENALLYTEM EERVRDRTRE LAESLSAVKT KGDQVSALLD NSGQGFLSFR GDLVVEPEFS HPCLTFFGGS PAGKPVDELL FSGNEHARDT LRACIEEALK EHDTSRAELY LSLLPEEISI GRRVLKAEFK PLNRSIMVVL TDITGEKALA AQVARERTRL EMIVSAVTYG NDFFDAVAEF TNFVQDGAGM WRGRDRAVLY RTIHTFKGTF NQLGFHHLPT QLHDVESSLQ RLGRRGDAAE AATMVFARDW QAVLNADLET VREALGDDFM ARRGVVTVTP EQAKRFERFA RGLLSETDIP NVLEEIAAIR TVSLRQAIAD FDKMIHQISA RLEKEVAPLV VEGDDVRIDP EVFGPFLRSL GHVFRNAIDH GIEDPDSRLS TGKSEIGTIT CAIRRNNGAL DIDIADDGAG IDVETLRRRA AELTSDDVSD WDIADLVFAE GISIRAEATE LSGRGVGMTA VKASVEELGG SIRIDSRPGH GTHFLFHIPF PPQVEGRAQ //