ID D3RQU3_ALLVD Unreviewed; 706 AA.
AC D3RQU3;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Alvin_2871 {ECO:0000313|EMBL:ADC63777.1};
OS Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB
OS 10441 / D) (Chromatium vinosum).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Allochromatium.
OX NCBI_TaxID=572477 {ECO:0000313|EMBL:ADC63777.1, ECO:0000313|Proteomes:UP000001441};
RN [1] {ECO:0000313|EMBL:ADC63777.1, ECO:0000313|Proteomes:UP000001441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D
RC {ECO:0000313|Proteomes:UP000001441};
RX PubMed=22675582; DOI=10.4056/sigs.2335270;
RA Weissgerber T., Zigann R., Bruce D., Chang Y.J., Detter J.C., Han C.,
RA Hauser L., Jeffries C.D., Land M., Munk A.C., Tapia R., Dahl C.;
RT "Complete genome sequence of Allochromatium vinosum DSM 180(T).";
RL Stand. Genomic Sci. 5:311-330(2011).
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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP001896; ADC63777.1; -; Genomic_DNA.
DR RefSeq; WP_012972042.1; NC_013851.1.
DR AlphaFoldDB; D3RQU3; -.
DR STRING; 572477.Alvin_2871; -.
DR KEGG; alv:Alvin_2871; -.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_390649_0_0_6; -.
DR Proteomes; UP000001441; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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; 2.
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 NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43047:SF79; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13426; PAS_9; 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 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:ADC63777.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001441};
KW Transferase {ECO:0000313|EMBL:ADC63777.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 326..372
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 399..451
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 469..692
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 706 AA; 77625 MW; ADD7A2DE13471BF0 CRC64;
MSHSESQRHG LILAALVLLA SGWLAAFGIT LWRLHDKATT DAFATARMHA RNFEDYLTKT
LQVIDLSVGN LPPGQDLTDD RALATHLTGL LRPSPFLRSL SILTTDGSVI GSSDARNIGL
RITLDGFYPE TTLGGAPPRI GRPWVGRDLA NATPSTGQPP PPRAASLIPV MHRFELDDTP
YWWLAALNPD DFIGHFSQLL PIEEGRVQLL RYDGLLLLST SPDDIPGRPD QSGAVPARLE
RQELGELAQT LADGHHVLTA YRASSRYPAV IAVHLDRGYI QAQWLREAGR LSMIVVPILA
ALSAAILLLW LRRRRLAQQR AELERQRRLT SSVFEASSDA IMLTTPSGEI LSTNPAFERM
TGYSGAEALG RNPRFLSSGL HDQTFYRDIW CAVITQGHWR GEIVNRRRDG ELYNALLTID
AVHDEYGELQ HYVGVTSDIT DRKRHEAELL AAKERAESAA RAKTTFLSTM SHELRTPMHG
ILGMTQLLLE SDLNERQRRQ LDTVKRSADT LLAILADILD YTRMDAEELQ LQPGPCDPLR
IIRDVMTVYA PQAEKKGLGF VLDSSRPAPG FVIVDARRLQ QILDKLTANA VKFTHEGEIR
LATWLDTETP AGGSGRLAIC VTDTGIGIPD ALHESIFEPF VQADGSHTRR YGGTGLGLAI
ARRLAEALGG TLSVESEPDQ GSRFTLSIPV QPIEIGRASS PSSNPS
//
