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Database: UniProt
Entry: A0L4N5_MAGMM
LinkDB: A0L4N5_MAGMM
Original site: A0L4N5_MAGMM 
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
//
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