ID A0A0U5MKN4_9PROT Unreviewed; 2127 AA.
AC A0A0U5MKN4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=XM1_3256 {ECO:0000313|EMBL:CUW40317.1};
OS Magnetospirillum sp. XM-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=1663591 {ECO:0000313|EMBL:CUW40317.1, ECO:0000313|Proteomes:UP000063191};
RN [1] {ECO:0000313|Proteomes:UP000063191}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wang Y.;
RL Submitted (DEC-2015) 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 -!- 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}.
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DR EMBL; LN997848; CUW40317.1; -; Genomic_DNA.
DR STRING; 1663591.XM1_3256; -.
DR KEGG; magx:XM1_3256; -.
DR PATRIC; fig|1663591.3.peg.3212; -.
DR Proteomes; UP000063191; Chromosome I.
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; 3.
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; 2.
DR Gene3D; 3.30.450.20; PAS domain; 4.
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; IPR013656; PAS_4.
DR InterPro; IPR018771; PocR_dom.
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; 3.
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; 2.
DR Pfam; PF08448; PAS_4; 2.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF10114; PocR; 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; SM00073; HPT; 2.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 4.
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; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 2.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 3.
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};
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}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 193..217
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 217..270
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 485..556
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 558..610
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 611..668
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 690..741
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 859..931
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1289..1510
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1527..1647
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1676..1791
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1833..1932
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 2022..2115
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT REGION 1795..1825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1244..1282
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1580
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1725
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1872
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 2061
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 2127 AA; 229279 MW; 0AE7988ABC5DAA85 CRC64;
MNRLLNTLER VSLRTKLLSG FAILLALTVL LGAVGLYNQN VLNKGSHRLY EIDLKGISHL
KDARVELAKM GRALRQAILA PDAGERERAI VLLNESEARL GLEIKDAQAH VIRDENKKNL
ASFEEQYRSY KASVDQTLAL LRKNSAEAAI AVASPEFQHL GVNADAALAL LSDYKEEQAR
IEVANASAAA EGAILLTLSL LAGAVAISLL AALAVTLSVR RPIDRLSAVV TELATGKLDL
DVPGTDLPNE VGALARAIDV LRADSRQMEE QRWVKTHLAA ISAELQTSAN PGELARKLFS
MLAPLLKLGQ AAFYVMDESG KHLSLQGGYA HRERKSLEQG FAVGEGLVGQ CALERSPIVI
TQPPADYIRI GGATGDMAPK SIAVVPVLRG DNLLAVVEFA TIEGFGPRDQ ALLDGIMPVL
AMSLEIIERT NKTQQLLAET QIQAATLAAS ERQIAARKQE LEVINDQLAE QGRLVEEQAG
ELGRERSLLR SLIDSIPDVI FVKDMLGVYL VGNQAFAEMI GKPLDAIVGK TDFDLFPPEK
ADQYRQNDVT MVAEGKTLTC EESGTYPDGR VAHFEATKVP LHSPDGTLLG LIGIARDITQ
RKSAELALAE AEERSRLILG SVSEGIAGLA PDGRITFINP AGAQMLGYEI ADLVGKGMHA
LVHHSYPDGK AFPRECCPMH LTSVDGAPRT VADEVLWRGD GTSFPVEYAT TPVMKDGQVV
GTVVSFRDIT ERKAAAEALI AERERLQNIL DKSPISIAIT VDGEIQFANP IVMEKFGFRV
GDYAPNVYVR QSDRDALLES LHRDGIVRNR EVQMWSVDKT PLDMLVTYLP IPFNGRTGIL
SWLMDITERK AAENAIRDQA AFQEALVDTI PYPLFYKGPD GRFLGFNRAY EQTFGVARQK
LIGKRVLDLD YLPESDRITY QAEDEAVIAN ASVVQKEMPI PFADGKVHDT LYYVSGFRKV
DGTAGGLVGT FVDVSDRKKV EEIERFNRLA LGREQRIIDL KRRINELALR LGLPPAFLSP
EQAEEADDTT SDVVVPQVLD GEAIRGAFVA LLRENELQSL FADFCEAVGI AAAIIDPQGD
ILAAARWQRA CTDFHRVNPQ SCARCIESDT ELALNLQEGK DYAMYRCRNG MTDCASPIVI
AGHHVANVFI GQFHTGSLDE AFFAAQADEL GFDRAEYLAA VREAPVIDEV RLPFILGFLA
RFAKLVGSFA VEQWKARQAE AAIRTHVVEA SRERVAAISL AEDAEHARAE VVEYKEHLED
LVEERTAELA IAKEKAEAAS QAKADFLANM SHEIRTPMNA IIGMSHLALK TELNPRQKDY
VRKIQQSGQH LLGIINDILD FSKIEAGKLA VERTEVHLDK VLDNVANLIT DKATAKGLEL
VFDVGADVPN DLEGDPLRLG QILINYANNA IKFTEKGEIT IRVRLGQDLG GEVVLRFEVR
DTGIGLTEEQ KGRLFQSFQQ ADSSTTRKYG GTGLGLAISK KLAELMGGSV GVESVPDKGS
TFWFTATLGK GKPRRKLLPK PDLRGRRMLV VDDNENARAV LVDMLSSMSF KVDDVDSGPA
AVDAIRNTAG GAPYEIVFLD WQMPGMDGIE TAYAIKGLGL PVTPHLIMVT AHGREEVMKG
AETAGIEEVL IKPVNPSLLF DSAMRSLGAV LEDEPDSVPD AAGVSAADLA GLKGLKVLLV
EDNDFNQQVA TELLADGGVV VEIAENGAVA VDKVRAGVYD MVLMDMQMPV MDGITATREI
RKMGHADLPI IAMTANAMQA DRDRCLEAGM NDHLAKPIDP DEMFATLLKW RRAAAPSPAP
SPAAPPSQPA AGDIPTDIPG LDTNAGLKRV RGKRPLYLDM LRKFATGQKN AVGDIGAALA
AGDLATAERI AHTLKGIAGN VGAAALQSLA ADVEAAIKAG KDSSAPLAAL APVLSELTGR
VAAALAPPEE APGPGGDAAG LIQRLRALLA DSDAEAEELV VNNLPLLRSA LGSRADSIAR
HVVDFDFDRA LGLLDDKPAA APPALPEIDP DVFDFERMGP VYKWDMGRLR PILAAFLDDA
AAKVGRITAE SDLAALREAA HGLKGTANTA GAVRLGRLAA DIEDAAKAGN AEGVAMLAPL
LPVTLDELRD ALASFNAENG NAEKGAS
//
