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Database: UniProt
Entry: A0L7Q5_MAGMM
LinkDB: A0L7Q5_MAGMM
Original site: A0L7Q5_MAGMM 
ID   A0L7Q5_MAGMM            Unreviewed;       729 AA.
AC   A0L7Q5;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   27-MAR-2024, entry version 110.
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_1489 {ECO:0000313|EMBL:ABK43998.1};
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:ABK43998.1, 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:ABK43998.1, 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; ABK43998.1; -; Genomic_DNA.
DR   RefSeq; WP_011713151.1; NC_008576.1.
DR   AlphaFoldDB; A0L7Q5; -.
DR   STRING; 156889.Mmc1_1489; -.
DR   KEGG; mgm:Mmc1_1489; -.
DR   eggNOG; COG4191; Bacteria.
DR   HOGENOM; CLU_379838_0_0_5; -.
DR   OrthoDB; 7818322at2; -.
DR   Proteomes; UP000002586; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 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; 1.
DR   InterPro; IPR045812; DAHL.
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; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
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; PF19443; DAHL; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:ABK43998.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002586};
KW   Transferase {ECO:0000313|EMBL:ABK43998.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        270..287
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          321..391
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          395..448
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          493..724
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   729 AA;  83132 MW;  6236B555AF342FB1 CRC64;
     MMRLTSNNIW VFIAVVAMGV VSLVTLLTFT RQIDQSQHRQ VQGHLQQLYR LDAAMDQSLG
     LVQHGMLTHY DSFVQYSLEI NQILKALDPA QARSGLSRSD EMVSLYQGLL KSWQEKLWLV
     ERFKSDQAVL RNSLRYFPQA LMEITEQLDH NKPELTGFDA NQARVMSRQL TLLLRLTLVS
     NNRGPEQDLW ALGQSQELIL TLLEQHQGTL VQQVRNLMEH GALIHKFQMK VNRWSQDAVA
     QPTERQLDRL AESYYAAFEG DLRRADQLRL WMYLLTLVLI GVGMLVARKV MLLRLAHAQQ
     EALVAQRTTE LRRELLERRK AEERFRSVAE SAGDAILAVD RHGRISFWNR SATTIFGYEY
     AQVKGRSLEM LVPEHQQSFY QHILQASLKA DALLKPREVQ TLEAQRADGT IFPVEASLAS
     WKTGGKRFFT LVIRDITERK AMEDRLHATL NSLDAKVAER TSELQSRMDE LNRTRDQLVS
     SEKMASIGRL AAGVAHEINT PIGIAVGAAS QNRETTNRIL AMLEQEEVDE ESLVEELKSL
     DKLAHLISNS MEKAAKLIRV MRRFTHISTD WQLEPLDMES ALLEIVDPLR PMFDQQHVVL
     QIKVEQALQV MSRKDLVQEI FSDLLNNTLV HAFPQPGGGE VKIVISYVEG EVLLNYQDDG
     IGMDEVVQQQ MFEPFFTTAH PEGRYGLGLY FLQTLVQGQL QGRVLCQSGT GEGVRFEICW
     PCERVLVQP
//
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