ID Q2W341_MAGSA Unreviewed; 1248 AA.
AC Q2W341;
DT 10-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 10-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 126.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=amb2930 {ECO:0000313|EMBL:BAE51734.1};
OS Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Magnetospirillaceae; Paramagnetospirillum.
OX NCBI_TaxID=342108 {ECO:0000313|EMBL:BAE51734.1, ECO:0000313|Proteomes:UP000007058};
RN [1] {ECO:0000313|EMBL:BAE51734.1, 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};
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DR EMBL; AP007255; BAE51734.1; -; Genomic_DNA.
DR RefSeq; WP_011385307.1; NC_007626.1.
DR AlphaFoldDB; Q2W341; -.
DR STRING; 342108.amb2930; -.
DR KEGG; mag:amb2930; -.
DR HOGENOM; CLU_265982_0_0_5; -.
DR OrthoDB; 9801651at2; -.
DR Proteomes; UP000007058; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
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; 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; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal 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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
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; PF13185; GAF_2; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13426; PAS_9; 1.
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; SM00086; PAC; 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; 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; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
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}.
FT DOMAIN 345..398
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 726..947
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 964..1084
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1111..1226
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 1017
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1160
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1248 AA; 134712 MW; 3988D91DA64EB3F3 CRC64;
MRVSTVVSLG MGLVILASMV LIGRVMAPHL DRQASIQSGR AAERLMELGL GAATRISAER
GPANGILGSD LPLPSDRVEA LRAAREVTDA ALHEVTAELN GRHPLRQSDV IALSLAESGR
QLAAARRQID TLASRPRAER NDAEVLAAVS AMVEVLPLLA PGLNVIENNL AQADPALINF
VTIARLATEM RDQAGQLGSV FTAPFVARRP MSVDELARIE RSLGIIQALD YQLRLALDKT
GSPPELKAAL AVIDAEFFGG GLPLARRIRD MGRTGGEYGM GAADFAKIYV PQMNVILGLR
GAALHSISAR MTGIEAESRS AMQITLGLAG IVFVSVLGCF LVIVRRMWHP LSQVNRALGQ
LARGEDRMDL PLVRRHDEIG EVVDSLTRLA AVVRERAEES HVSGLVAKIT SGLQSAEDLA
SLSQVLFTHL EPILHLGFAG YFRLDDQARA LLSCGGYARD GEASPPGRVE LGDGLVGECA
LEKREILIAD PPPGYVRART GLLSALPRAV LILPVLSGGQ CLGVIELAML QPLGGTGRRV
LDDVLPLLAM RMEILARTER TQQLLAATRE LAETLEANQT EIQSLLSEQQ AIFEAATVGI
AFLKNRVIVR GNPRLDKLFG YGPGELVGQS TRIWFADDAA FADVGGAYEA LSRGEVHQRE
QEYLRKDQSR FWCRISGSAI DPSDLSRGTV WMLEDVTQAR ATAEAQARAK DAAEDAARTK
SDFLANMSHE IRTPMNAIIG MAHLALKTDL DPRQKDYVRK IQQSGQHLLG IINDILDFSK
IEAGKLEVEA TEIHLDKVLE NVGNLISEKA TAKGLELLFD VGAGVPLDLM GDALRLGQVL
INYANNAVKF TEAGEIVVAV RLMEDLGPDV MLRFEVRDTG IGLTDEQKAR LFQSFSQADT
STTRKFGGTG LGLAISKKLA ELMGGSVGVD SVPGQGSTFW FTARLGKGKP RAPLIPEAEL
QGRRMLVVDD NENARAVLVD MLSAMSFEVD AVDSGAKALD AIRDAVLDLP YDVVFLDWQM
PDMDGLEVAE QIHSIRLPFP PHLIMVTAYG REEIIKGAQA ADIGEVLIKP VSPAALFDSI
MRVFASDQRR DEAEDVSEGG SVDHAALRGL KVLLVEDNDL NQEVAGEILR DAGIEVEIAD
NGLIAVEKAR AGVYDLILMD MQMPVMDGVT ATREIRRLGH VDLPIIAMTA NAMQADRDKC
LEAGMNDHIA KPIDPDTMFS TISRWCAAEP PRRAGTASDG CATKVDGR
//
