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Database: UniProt
Entry: C0QH28_DESAH
LinkDB: C0QH28_DESAH
Original site: C0QH28_DESAH 
ID   C0QH28_DESAH            Unreviewed;       772 AA.
AC   C0QH28;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=HRM2_25830 {ECO:0000313|EMBL:ACN15677.1};
OS   Desulforapulum autotrophicum (strain ATCC 43914 / DSM 3382 / VKM B-1955 /
OS   HRM2) (Desulfobacterium autotrophicum).
OC   Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC   Desulfobacteraceae; Desulforapulum.
OX   NCBI_TaxID=177437 {ECO:0000313|EMBL:ACN15677.1, ECO:0000313|Proteomes:UP000000442};
RN   [1] {ECO:0000313|EMBL:ACN15677.1, ECO:0000313|Proteomes:UP000000442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43914 / DSM 3382 / HRM2
RC   {ECO:0000313|Proteomes:UP000000442};
RX   PubMed=19187283; DOI=10.1111/j.1462-2920.2008.01825.x;
RA   Strittmatter A.W., Liesegang H., Rabus R., Decker I., Amann J., Andres S.,
RA   Henne A., Fricke W.F., Martinez-Arias R., Bartels D., Goesmann A.,
RA   Krause L., Puehler A., Klenk H.P., Richter M., Schuler M., Gloeckner F.O.,
RA   Meyerdierks A., Gottschalk G., Amann R.;
RT   "Genome sequence of Desulfobacterium autotrophicum HRM2, a marine sulfate
RT   reducer oxidizing organic carbon completely to carbon dioxide.";
RL   Environ. Microbiol. 11:1038-1055(2009).
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; CP001087; ACN15677.1; -; Genomic_DNA.
DR   RefSeq; WP_015904441.1; NC_012108.1.
DR   AlphaFoldDB; C0QH28; -.
DR   STRING; 177437.HRM2_25830; -.
DR   KEGG; dat:HRM2_25830; -.
DR   eggNOG; COG3850; Bacteria.
DR   eggNOG; COG4191; Bacteria.
DR   HOGENOM; CLU_000445_89_29_7; -.
DR   Proteomes; UP000000442; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.290; -; 1.
DR   Gene3D; 6.10.340.10; -; 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; IPR003660; HAMP_dom.
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; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF13426; PAS_9; 2.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF158472; HAMP domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ACN15677.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000442};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        203..223
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          224..276
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          350..402
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          403..458
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          536..761
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          264..291
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   772 AA;  87632 MW;  DC1B1FA146F013CC CRC64;
     MKRTPDMLLN KIRHSLVFKL IMIMAFICFV AISVWAYFSI NYQRNKAVGD TLGVADRISK
     TIRLGTHYSM MLNARDDIHQ IIQNTATQRE IENVRIYNKR GVIKFSNIES EVDTKSLPES
     EACIICHRGD PPLVKLTLNE RKRIFSADSG HRVLGIITPI YNEPGCSEQC HFHDAKAKVL
     GSMELVISLQ ETDAEIVKYE QSIVFLALAI FVAPSFFIFL FVYKFVIGPI RQLTEETKHI
     TCATKITRID SHRESEIGQL ATAFNTMRQR INHHQKELTK QKNEYQNLFE RVPCLITVQD
     KNFKLINFNK EFYNKYNPKI GDFCYATYKG RTTRCSNCPV EKTFKDGKSH YSEEEGIGKN
     GTMEHWIVRT SPVKNAAGEI VAAMEINLDI THRKELEQRA ELSEKKYHAI FNNIPNPVFV
     LDNDSLTILD CNESVAEVYG YGMADIVGKP FSYLFDPSQP TQEIDDIVRN TSIINSVKHR
     RSNNRPMFVD IWISPSEYPG QKVLLVTTSD ITQRLETETQ FLQAAKLATL GEMATGVAHE
     LNQPLSVIKT ASSFCIEKIR KNQEINPEIL TTLLQKIDAN VNRASKIINH MRDFARKSDI
     KLIPVDIVDI LERAYEIFSQ QLKVRGITVD WDITPPLAPV MTDPGRLEQV FINLLINARD
     AIEAKAEICH NDAGLKKKIT IRGYLLDEKV HVEVEDTGTG VPADVAEKIF QPFFTTKEVG
     KGTGLGLSIS YGIIKESSGL ISIKETSEKG AVFQVILPAY RSKEQDNHEE RS
//
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