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Database: UniProt
Entry: A0A1M6JBF7_MALRU
LinkDB: A0A1M6JBF7_MALRU
Original site: A0A1M6JBF7_MALRU 
ID   A0A1M6JBF7_MALRU        Unreviewed;       876 AA.
AC   A0A1M6JBF7;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN02745165_02379 {ECO:0000313|EMBL:SHJ44003.1};
OS   Malonomonas rubra DSM 5091.
OC   Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Desulfuromonadales;
OC   Geopsychrobacteraceae; Malonomonas.
OX   NCBI_TaxID=1122189 {ECO:0000313|EMBL:SHJ44003.1, ECO:0000313|Proteomes:UP000184171};
RN   [1] {ECO:0000313|EMBL:SHJ44003.1, ECO:0000313|Proteomes:UP000184171}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5091 {ECO:0000313|EMBL:SHJ44003.1,
RC   ECO:0000313|Proteomes:UP000184171};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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; FQZT01000008; SHJ44003.1; -; Genomic_DNA.
DR   RefSeq; WP_072908955.1; NZ_FQZT01000008.1.
DR   AlphaFoldDB; A0A1M6JBF7; -.
DR   STRING; 1122189.SAMN02745165_02379; -.
DR   OrthoDB; 9761263at2; -.
DR   Proteomes; UP000184171; Unassembled WGS sequence.
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; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 1.
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; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR001610; PAC.
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   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
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; PF00512; HisKA; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   Pfam; PF12974; Phosphonate-bd; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 1.
DR   SMART; SM00091; PAS; 1.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 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.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000184171}.
FT   DOMAIN          370..416
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          441..495
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          508..731
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          751..867
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         802
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   876 AA;  97718 MW;  8CA4D16448152591 CRC64;
     MLHAFPSHRQ KSKFVTRGSS LLRYLCIIFA LLLLVSLAHS HPAPPVKIGV LAKRSIFADF
     QKWAATASYL SGTIHDRRFE IIPLDFENVR LAVMAGDIDF LITNSSYYVT LEADHGLQRI
     ATLVNLHDKE PRQMFGGVVF TRADRSDIST FKDLIGKHFW AVDQNSLGGW LAAWREFHAQ
     GINPERDFGL LKFSGTHDEV VHAVFNGEAD AGTVRTDTLE RMAFEGEISL DEVKVLNQQA
     GDSKFDYLCS TRFYPEWPFA ALKHTPKRLV EQVTLALMAM PTSSHAAQTA NIAGWTAPLD
     YQSIHELLKD RHLFLHEKYV GKPTLSTFLK QHWQAGVLVI ICICLLSYVA VYKSRLNRQL
     ESRIANRTQA LNRLASAVEQ SGETIVITDA EAKIEYVNSA FTTVTGYRRD EVIGKNPRIL
     NSGEQDDAVY ADLWQTISHG KSWKGRFANK KKDGSRFVED VNISPIINSE GEIVNYVAVK
     RDITEQLQIE EQYRQSQKLD AIGKLAGGVA HDFNNMLAII LGQVELLLMK TEADNPLRQR
     LLEIKNASTR SSELTQQLLG FARKQPHTPR ILNLNEAVTT TLNMLKRLIG KHIDVRWRAE
     TEKAFVKIDT GHLNQILTNL IINARDAIDG NGSISIRTAH ASLDEKFCQE HLGTKPGEFI
     LVEISDTGCG MNKEVLSKIF DPFFTTKDPS KGTGLGLSMV FGLVKQNNGY IYVQSSEGQG
     ATFSLYFPAV ASEIKDPALI ENHELVHGSE TILVVEDEAS ILEIARSFLT EAGYNVLSAQ
     VPEEAIKLAN NHLGTIELLL TDIIMPKMSG VELGEALLKK HPHLKILYMS GYSGEHLIPK
     SDAATEPDVL LKPFSAHSLT KKIRAILDSK TSTERI
//
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