ID A0LC29_MAGMM Unreviewed; 807 AA.
AC A0LC29;
DT 12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT 12-DEC-2006, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Mmc1_3031 {ECO:0000313|EMBL:ABK45522.1};
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:ABK45522.1, 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:ABK45522.1, 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; ABK45522.1; -; Genomic_DNA.
DR RefSeq; WP_011714586.1; NC_008576.1.
DR AlphaFoldDB; A0LC29; -.
DR STRING; 156889.Mmc1_3031; -.
DR KEGG; mgm:Mmc1_3031; -.
DR eggNOG; COG3852; Bacteria.
DR HOGENOM; CLU_000445_114_64_5; -.
DR OrthoDB; 7340865at2; -.
DR Proteomes; UP000002586; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 3.30.450.290; -; 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; 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; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR021796; Tll0287-like.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF11845; DUF3365; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08448; PAS_4; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00086; PAC; 2.
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; 2.
DR PROSITE; PS50112; PAS; 2.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ABK45522.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000002586};
KW Transferase {ECO:0000313|EMBL:ABK45522.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 221..238
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 261..331
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 337..389
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 390..444
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 468..518
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 640..792
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 807 AA; 90011 MW; 98BD8B964E871263 CRC64;
MKSFIPNATA GVSFFPTMKM AILWSLLMLL LVAGSLFEIK QDMQRLALSQ ARTALERDLD
FRYWASMHGG VYVPMTKITP ANPFLAHVDE RDISTPSGRQ LTLMNPAYML RQIYQVIRDN
GDIQGHLTSL KPLNPGNYAD PWEMSALKHF EQGETEVADF LQKDGKSVLR LMQPLITEEG
CLKCHAHQGY KLGDVRGGLS VTIHMLPWET MGRQHVLRQG SVIFAIWIIG MFGLWLLGRR
IHQETARCWN AETESKQVVL ERNKAKQYLD IVGSIIVKLD RDGIVELINN KGCTVLEYSR
EALLGKNWFD KVSPSDVREQ QRKIHTAVCL GQIEGAEYVE SAAVTKSGQR RMLAWHHTLV
KDDEGQITGS LSAAEDITEQ IKMTQALQES IERTRMIAQA AQDAIIMIDE FGRVSFWNAA
AERIFGHAES EVLGQDLHTL VAPKRYHESF KRGFAQFAMT GSGAAVDKTL ELTALRKDGS
EFAMEISLAA VPHGDNWHAV GVVRDISDRK RAEEREQHAS FQAGVAEMSI SILHNIGNAI
MSIMNRSERI TSASEALAHT AELFDRVGRS VALKREKGQS DTQILTGLLP AFEEISTKLA
NMAKADFMEN AAAIHQGVFH ISEIIKIHQD SAQHTMVTRF DLASLIDDAI MIQSDSLDKY
DIEVQLNFTQ TLEQVALPRS QLLQLIINLI KNSREAIVTR FQDHDEKGQI IVSVEQKERA
WLEIRVQDNG CGIATDKLAE TFRFGYTTKE KGTGFGLHSA ANFVQSIGGE IVCQSEGLGR
GALFIVTLPM EILPNEAGAN HPIVKEG
//
