ID A0A178MR52_9PROT Unreviewed; 1750 AA.
AC A0A178MR52;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=A6A05_12340 {ECO:0000313|EMBL:OAN50555.1};
OS Magnetospirillum moscoviense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=1437059 {ECO:0000313|EMBL:OAN50555.1, ECO:0000313|Proteomes:UP000078543};
RN [1] {ECO:0000313|EMBL:OAN50555.1, ECO:0000313|Proteomes:UP000078543}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BB-1 {ECO:0000313|EMBL:OAN50555.1,
RC ECO:0000313|Proteomes:UP000078543};
RA Koziaeva V., Dziuba M.V., Ivanov T.M., Kuznetsov B., Grouzdev D.S.;
RT "Draft genome sequence of freshwater magnetotactic bacteria
RT Magnetospirillum marisnigri SP-1 and Magnetospirillum moscoviense BB-1.";
RL Submitted (APR-2016) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAN50555.1}.
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DR EMBL; LWQU01000138; OAN50555.1; -; Genomic_DNA.
DR RefSeq; WP_068500305.1; NZ_LWQU01000138.1.
DR STRING; 1437059.A6A05_12340; -.
DR OrthoDB; 9801651at2; -.
DR Proteomes; UP000078543; Unassembled WGS sequence.
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; 2.
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; 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; IPR013655; PAS_fold_3.
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; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF13426; PAS_9; 2.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00086; PAC; 4.
DR SMART; SM00091; PAS; 2.
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); 4.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 4.
DR PROSITE; PS50112; PAS; 2.
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}; Reference proteome {ECO:0000313|Proteomes:UP000078543};
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 196..220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 218..271
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 472..526
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 550..602
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 603..679
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 681..733
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 816..870
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 953..1006
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1024..1245
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1264..1387
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1415..1532
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1575..1669
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 90..117
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 431..472
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1318
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1465
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1614
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1750 AA; 190340 MW; D4E3876049150AC1 CRC64;
MKVILTAIGQ WPLMRKMLLG LSSIVAVALG INLYSLYSMN QISRTFDRFY ANEIATLSHL
KEARVQYAFM GRALRQAILP QAPGERDTAY RQLADAESGL RREMDEARKR LDLESNKAAL
ARFDAALNQY KLRVELVVAA QRRGDLADSL ALLAAPEFQQ AGRAANDALA EIAKGTEVVA
QMTATAARTR SEDAMVFALA ILGGGLILAL GLGIVITWSI RGPSEHLRLA VDKLADGHLD
VTVPHTDYPN EIGGLARSIE VLQAQSRQLA AQRWVKTNQA AIGSQLQAAT DITDLARGFL
ARLAPLLNIG HGVFYCHVEA ERHLRLVGSY AFLARKTFNQ TIALGQGLVG QCALERQPII
ITEPPEDYVR ISSALGEAVP RAIMALPILH NDQLMGVVEL ATFERFGPDQ ESLLEGVMPI
LAMTMEILER NAKTQELLAE TRRQAENMEK QAARLEEQSV ELEAQQTEIK ATEAWYRGII
ESAPDGMLVT DESGAIVMVN PQVEAMFGYG PGELAGRPIE VLVPESARGG HAAQRDGFIH
SDDRARVAMR DRELRGVRKD GAEFPVEVGL SRLPAIGGRG RCICASIRDI TARKVAEDRM
AILEERSRLI LGAVQDGIVG LDNDGIIVFA NPAASALLGY TPDEYQGMGM HALVHHHYPD
GRDFPRDECA MYKTSVDGQP RTVDSEVLWK KDGTALPVEY STTPVIKDGV LKGTVIVYRD
ITERKRLQEE MKRANFLSDV ALELTGSGYW QVDYSDPDYY YQSDRAANIL GEPLKPDGRY
HLMDEWFSRL QEANEETARL TAERYQGAID GTYDHYDSTY AYKRPVDGKV VWVRAAGKLV
RDDASGKILY MYGAYQDITE RKRAEDEIKH INMLSDSALD LTKAGYWLID YSDPDYYTSS
ERAAAIFGEI PTPGFRYHLM DEWYSRITAA DPAVAEATGL HYADAVAGKV PRYDTTYCYK
RPMDGQIAWI RAIGNVVRDG NGNPLFMYGV SQDVTEIKQA EAAVLRAKEI AEEATKAKSD
FLANMSHEIR TPMNAIIGMS HLALQTKLDK KQRNYIEKVH RSGENLLGII NDILDFSKIE
AGKMSMEAID FHLEDVMDNL AGLVGLKAED KGLELLFNIA PNIPTALVGD PLRLGQVLIN
LGNNAVKFTD KGEIIVGAEM VNRADDRVTL HFWVHDSGIG MTPEQCGKMF QSFSQADSST
TRKYGGTGLG LAISKNLVEM MNGRIWVESE AGKGSTFHFE VHLGVQSQPA PRRTFRPDEL
KGLRVLVVDD NASAREILSV MAKGFGLEVD AAWDGRQALD MIAAANKREL TYDLILMDWK
MPIMDGVETV QHLQADPGAN IPAVIMVTAY GREEALTDAQ ERGIALKTVL TKPVTAASLL
EAVGETLGKG VVVETGTQDK AAGYQAAMKA LDGVRVLLVE DNEMNQELAT ELLSQAGMEV
VVAVNGQEAL DILAGDSRFD GILMDCQMPV MDGYTATRLI RANPALAHIP VVAMTANAMA
GDRDKVVEAG MVDHIAKPLN LDTMFATMAK WIKPGRTVVP QSVEKPVPVP APVVGGLPDL
PGIDVKAGMA TMANKESLFL RMLAKFRDGQ AGFAQAFAAA RVDADPTAAT RAAHTLKGTA
GNIGAKGVQQ AAANLEQACK ENRPAVEIDA LLAVTLAELA PVVAGLGRVG GTAETPAKPA
ATADTEVKAT LGRLAALLRD SDSEAGDVLK ALILKIAGTD LAKALRPVAA AIEDCDLDGA
LEKLTAAGLP
//
