ID A1BID0_CHLPD Unreviewed; 985 AA.
AC A1BID0;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Cpha266_2152 {ECO:0000313|EMBL:ABL66157.1};
OS Chlorobium phaeobacteroides (strain DSM 266 / SMG 266 / 2430).
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=290317 {ECO:0000313|EMBL:ABL66157.1, ECO:0000313|Proteomes:UP000008701};
RN [1] {ECO:0000313|EMBL:ABL66157.1, ECO:0000313|Proteomes:UP000008701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 266 {ECO:0000313|EMBL:ABL66157.1,
RC ECO:0000313|Proteomes:UP000008701};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.,
RA Schmutz J., Larimer F., Land M., Hauser L., Mikhailova N., Li T.,
RA Overmann J., Bryant D.A., Richardson P.;
RT "Complete sequence of Chlorobium phaeobacteroides DSM 266.";
RL Submitted (DEC-2006) 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};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP000492; ABL66157.1; -; Genomic_DNA.
DR AlphaFoldDB; A1BID0; -.
DR STRING; 290317.Cpha266_2152; -.
DR KEGG; cph:Cpha266_2152; -.
DR eggNOG; COG0642; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_114_15_10; -.
DR Proteomes; UP000008701; Chromosome.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 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; IPR036641; HPT_dom_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 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; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ABL66157.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000008701};
KW Transferase {ECO:0000313|EMBL:ABL66157.1}.
FT DOMAIN 334..555
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 574..698
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 725..844
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 886..979
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 55..85
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 286..317
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 631
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 774
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 925
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 985 AA; 110327 MW; 4254AB81745D97F3 CRC64;
MQKPEYHDLQ QRILELETDS LRSRRIEQEL LEKQAVLGHQ NIKLIRKSIE LSDVKRQLED
NNYELEISQA KLQNALNSLR ESENTLSSVL VNSPDTIIAV DRDHRIIYVN RAMPGHKKTL
AVGDHLCDHI MQPYHDRYHH TIERVIVTGK TAVLECELVV SPEETIELES RFAPCFLNGE
VTSVVMLSVD ITERKGMELE LKKTLIDLER FNRVMVGREL RNIELKKRIA SLQNDLVLSS
GNAQASDDSR QDFATEDEDC AGIHHGDGFE EACDEVQYRK QQRMALLNLI EDANLARNEL
LETNRKLEES VIRTQEMARA ASKANEAKSQ FLANMSHEVR TPMNGVIGMS DLLLDTSLDP
EQRKYVETII SSGKNLLSII NDILDFSKIE ANRLDLDVVD FDLLELLEDV CGILGLQAQQ
KGLELTLVTG SFLPRFLRGD QARIRQILVN LVGNAVKFTH SGEVVVCAMA QEERDSQVTI
RLLVRDTGIG IPREMMKAVF EPFIQADGST RRKYGGTGLG LAISNQLAKK MGSTIILEST
NGEGSVFWFD VVLEKQCQSS ELLPESGAGL AGKRVLVVNR NASMRFMLKG VLESCSVDCT
VFGGIEEALA AVTSSSVHLE SVPVWNVAIL DTNVAEHSLE EFQRLIGTIT EVHRCPIILL
VSFGQYEEMK KLFSTGVFRL LLKPVRQAEV VVAVVDALNN ESAEYQEPVK QVGAGWQDSE
TETYHILLVE DSPVNQQVAV AMLRKIGYSP DVVASGKAAI DAMRCKVYDL VLMDCQMPEM
DGYEATRIIR TDRTLCGTPD IPVVAMTAHA MIGDREKCLS AGMDDYLPKP VCKSDLNAVL
LKYLQRKKKP EKIVEQKTCI AEVKSELITA DEVFLIDDLL WRMQNDREFV RMILGQFIGE
VPKRIVEMET ALDRHDTDLA SMIAHTIKGE AVTVGGKVLG LHASSIEMAA KSGDIKKSRE
FLRDLKEQFR IFIERVSATG WYAAE
//
