ID A0LC28_MAGMM Unreviewed; 801 AA.
AC A0LC28;
DT 12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT 12-DEC-2006, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Mmc1_3030 {ECO:0000313|EMBL:ABK45521.1};
OS Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Magnetococcales;
OC Magnetococcaceae; Magnetococcus.
OX NCBI_TaxID=156889 {ECO:0000313|EMBL:ABK45521.1, ECO:0000313|Proteomes:UP000002586};
RN [1] {ECO:0000313|Proteomes:UP000002586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1
RC {ECO:0000313|Proteomes:UP000002586};
RX PubMed=19465526; DOI=10.1128/AEM.02874-08;
RA Schubbe S., Williams T.J., Xie G., Kiss H.E., Brettin T.S., Martinez D.,
RA Ross C.A., Schuler D., Cox B.L., Nealson K.H., Bazylinski D.A.;
RT "Complete genome sequence of the chemolithoautotrophic marine magnetotactic
RT coccus strain MC-1.";
RL Appl. Environ. Microbiol. 75:4835-4852(2009).
RN [2] {ECO:0000313|EMBL:ABK45521.1, ECO:0000313|Proteomes:UP000002586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1
RC {ECO:0000313|Proteomes:UP000002586};
RX PubMed=22581902;
RA Bazylinski D.A., Williams T.J., Lefevre C.T., Berg R.J., Zhang C.L.,
RA Bowser S.S., Dean A.J., Beveridge T.J.;
RT "Magnetococcus marinus gen. nov., sp. nov., a marine, magnetotactic
RT bacterium that represents a novel lineage (Magnetococcaceae fam. nov.;
RT Magnetococcales ord. nov.) at the base of the Alphaproteobacteria.";
RL Int. J. Syst. Evol. Microbiol. 0:0-0(2012).
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; CP000471; ABK45521.1; -; Genomic_DNA.
DR RefSeq; WP_011714585.1; NC_008576.1.
DR AlphaFoldDB; A0LC28; -.
DR STRING; 156889.Mmc1_3030; -.
DR KEGG; mgm:Mmc1_3030; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG3829; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_114_51_5; -.
DR OrthoDB; 9789238at2; -.
DR Proteomes; UP000002586; Chromosome.
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; cd00130; PAS; 3.
DR CDD; cd00156; REC; 1.
DR Gene3D; 2.10.70.100; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
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; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 3.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 3.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ABK45521.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000002586};
KW Transferase {ECO:0000313|EMBL:ABK45521.1}.
FT DOMAIN 10..126
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 141..211
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 212..267
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 344..396
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 397..449
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 469..519
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 610..793
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT MOD_RES 59
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 801 AA; 89543 MW; F2B454F860D8EFA8 CRC64;
MSGSCGKKLK ILCVDDNKDF PAFLQHRLAH DGFEWVWVQE QGAILAEVQA GAYDAILIDY
HLKGSEDGID LLRRLLQEGD NVPPVIMVAH EATVQVAVTS IRLGATDFVY RDDGANFADF
LSKTLHNAIN KSSLMDAMAR SERRFKALVE SSNDWIWAVD AEGVYTYSSP MVEQMLGYSP
AEMMGKTPFD LMPHDEAQRV RANFQVLVEQ RRPIEKLVNR NRHKNGHLVV LESCGVPIFD
EEGHFAGYQG VDRDITDRVI LEEQNEKIRA RLERAQQLAH LGSWDWDYAT NLLTCSDEVY
RIFERPLQPQ AMPAEQFLEV VHVKDRALVH EALQRAFADP NDIYDIEYRI RRPAGDVRVV
RAKGDVVRDA AGKALRMVGT VQDITEIKQA EWALEEARDA WKRTFNAITE PILIVDTHYK
IVRCNRAMAK VLGISQQKIQ GMPCYEALHG VKEPFEACPH GQLLSQSCPN SKVLLEARLG
GNYEVSVYPI HAVSGELTGS IHIAHDLTER KKAEEKERYA SFQAGVAEMS VSILHNIGNV
IMGIMSRSDM IGDSSKELKA LAGLFGRVGE SIQNKRAQGK GEGDILNGVL SIFDELSSRL
AKMSNLDFTD NAEKIRTGIQ HISEIIKIHQ DASHYMLLTH FDLRDLLNDA VLIQADKLEK
FHIELTLECE DGLENIYLPR SQLLQLVINL IKNSQEAIGQ RLSTDPAAGW IHIVARRDEG
GGLMLQVQDN GCGIAPEQVA HVFRFGYTTK NRGTGFGLHS AASFVQSMQG KLEVESAGIG
QGCLFRLHLP LTGEDVKHAD Q
//
