ID V6EWV9_MAGGM Unreviewed; 1444 AA.
AC V6EWV9;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=MGMSRv2__0535 {ECO:0000313|EMBL:CDK97750.1};
OS Magnetospirillum gryphiswaldense (strain DSM 6361 / JCM 21280 / NBRC 15271
OS / MSR-1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=431944 {ECO:0000313|EMBL:CDK97750.1, ECO:0000313|Proteomes:UP000018922};
RN [1] {ECO:0000313|EMBL:CDK97750.1, ECO:0000313|Proteomes:UP000018922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1
RC {ECO:0000313|Proteomes:UP000018922};
RX PubMed=24625872; DOI=10.1128/genomeA.00171-14;
RA Wang X., Wang Q., Zhang W., Wang Y., Li L., Wen T., Zhang T., Zhang Y.,
RA Xu J., Hu J., Li S., Liu L., Liu J., Jiang W., Tian J., Li Y., Schuler D.,
RA Wang L., Li J.;
RT "Complete genome sequence of Magnetospirillum gryphiswaldense MSR-1.";
RL Genome Announc. 2:e00171-e00114(2014).
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; HG794546; CDK97750.1; -; Genomic_DNA.
DR STRING; 1430440.MGMSRv2__0535; -.
DR KEGG; mgy:MGMSRv2__0535; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG2770; Bacteria.
DR HOGENOM; CLU_003424_0_0_5; -.
DR Proteomes; UP000018922; Chromosome I.
DR GO; GO:0016020; C:membrane; 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; cd00130; PAS; 2.
DR CDD; cd18774; PDC2_HK_sensor; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 6.10.340.10; -; 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; 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; IPR036641; HPT_dom_sf.
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; 1.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF08447; PAS_3; 2.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 1.
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; 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); 2.
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; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000018922};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 336..358
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 359..412
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 442..518
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 573..648
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 649..701
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 719..940
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 958..1079
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1109..1225
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1265..1359
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 1012
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1158
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1304
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1444 AA; 158939 MW; 951A981BB19366D0 CRC64;
MTGTSVRTSL LLRAFAIVVM ALGVFAVSTY ALIVVPAIDR LAQSQMTQTA GELDSRVQRL
LATVEITLNT SRRWGVNGSL QLDQVERFNE FFFPMIENHP EISSVIFAHE SGREILLLHT
ADGKWINRLS DPDRWGNKTT WMTWSNTRVL EKTEILERDY DARKRPWFQG AMAMAEDLGV
FWTAPYIFFT TKEPGITAAS RWTGADGSRF IIAHDVKLLD LSHFTRGITA GPNGIGMLLD
DQGRLVGVPR DQRFDDDGEI KKSVLQPLAD AGLPVLAASW QHWNDLGRPN GSLNALEYRG
EEWFSHFRRV FIGQQSFWLA VVAPHRDFIP ISGDQTVLLV LLIVATLVAA TLVTLPIARR
FAAPLEHLAE ESTRIGRLDL QRPVAVASDL AEISALATAQ EAMRQALLAS TSRLEEANAT
LEARVSERTW ELEQSKGAAE WSRQLLREMA DSLPCATFRF EVVPGRSPAF RFVSAQVARI
LGVTAAELMN DPGLRLKNLH PDDLEPARIA QAEAIDRGQP TNLLYRVVLG NTAPRWIETR
SMVSESFDGT RVWNGYWLDV TEREEALARI RMAEERLRAL TDSVPVAVFE MRSQGDLFWF
TFISRKVREI LGIGRDELRA NAGRLYGTVA AADRDGLEES VVAAIGGGLH FSASFRLDSP
GDERWIRMEA VPIPGEQGDR VWAGFFQDIT AVKQAEAELT RAKELAEDAT RMKSDFLANM
SHEIRTPMNA IIGMSHLTLK TPLTPRQHDY VKKIQGAGQH LLGIINDILD FSKIEAGKLT
VEHIGFDLDK VLDNIASLLT EKTNAKNLEL VFDVPSDVPR ALVGDSLRLG QILINYANNA
VKFTEKGEID IIVRVQERTQ TEVVLYFAVR DTGIGITPEQ KARLFQSFEQ ADTSTTRKFG
GTGLGLAISK KLAELMDGAV GVESEYGKGS TFWFTARMGV GVERDRKLLP SPDLRGCRVL
VVDDNDNARA VLCDLLTSMT FEPSEVASGP AAVAEVKRAA DAGIPYALVL VDWRMPDMDG
IDTARHIRAL GVEHAPRLLM VTAYGREEVL NQINEAGIDD VLIKPLSASI LFDTVMRMFG
GGRNGESGAD DQGGSPAPLD DLAAIQGARI LLVEDNDLNQ EVAAELLADA GFVVDIADDG
AIALDKVQRN TYDIVLMDMQ MPVMDGVTAT REIRKLGRFD DLPIVAMTAN AMRRDQDLCR
DAGMNDFVAK PIDPDQLWAA LVRWIKPRHG SAATNAGPVA ATGPEHVPDI PGLDGVTGLR
RVQGKTSRYL MSLRKFAAGR RGAATDIRRA LDDADWTTAE RLAHTLKGLA GMIGAEQIQH
LAAALETALA DRMPRDVVDG LLTRLEQPLA ALVAALDECL PPEPEIVAAT AVDLKLVGEV
SDRLRKLLAD DDAMADDVLE ENAALLRAAF PEEYRRIHAG IKSFDFDVAL AALDRAMGRN
RRDA
//
