ID A0L4N5_MAGMM Unreviewed; 789 AA.
AC A0L4N5;
DT 12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT 12-DEC-2006, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
DE Flags: Precursor;
GN OrderedLocusNames=Mmc1_0402 {ECO:0000313|EMBL:ABK42928.1};
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:ABK42928.1, 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:ABK42928.1, 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; ABK42928.1; -; Genomic_DNA.
DR RefSeq; WP_011712098.1; NC_008576.1.
DR AlphaFoldDB; A0L4N5; -.
DR STRING; 156889.Mmc1_0402; -.
DR KEGG; mgm:Mmc1_0402; -.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_355559_0_0_5; -.
DR OrthoDB; 7325042at2; -.
DR Proteomes; UP000002586; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
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; PF08448; PAS_4; 1.
DR Pfam; PF13188; PAS_8; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ABK42928.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000002586};
KW Transferase {ECO:0000313|EMBL:ABK42928.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 187..209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 388..458
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 461..513
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 558..789
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 789 AA; 88275 MW; 8DD9D10D613DC6DA CRC64;
MSIRTQIVTL LLLFALLVAG LYGWVLNRHN NDALLFAADQ KLGAAAALVA QILPVEYHDH
IEGADSVSQK KYQSIVQNYN RLCQELKLDG MWSVLWLDKQ PYLTSSTSRS LVLQQGDYPP
FFAPHPHPEL FSENTTTPDY RTITQKGVPL RMIQLPQLDK RGRLYIIGAT LPLLPLQEAL
LETVSPALTL VLVFFTLLLL FGFLGSAWIS QPLQQLVRLA PQQTARAALV MLERTGSPEV
ETLLASLNAL SKDFTDQCAL NRTYQHLSYA MDTSPIATAI LDNRGRLLYA NARFRAAAGG
QELTQPGAHM DQFQLGFPAA LDRSWRKHVS LSQPWAAEVE TNVSGAASGY ERVTITPFRN
SNHAEHAILF TLQNVARRKK LEQELRHEIN FQRVLMNTLP IPVFFKDTQG VFLGCNAAYC
TLLGMAEWEI VGRTIFQILP NEAASFYHKK DNLVLQGGGL LDYEGYLRNS TGQERLLHLF
TAPFHNADRS LAGLVAAIVD ITDRVLFESK IMQMNADLEL RVVERTRDLE ESMESVQRLQ
RLLVETETMA TLGTMVAGVA HEVNSPLGVG VMASSELQQE VAKFRKTYET EGISEEEFEG
FIHRSEDLLG LTVTNLRRAG ELLQNFKRVA VDQSDEAQHV FQLDEQIEAV LHALSYLFRK
RAIQMRLECP KGLTIKSLPG AVSQIVTNLI SNAIKHGFDV GMRGTITLTV KRHDQQIILD
FYDDGKGMDQ ETQEKIFERF FTTQRGSGGS GLGMHIVQSL VVQKLRGSIH CESELGKGTR
FVVTFPVEA
//