ID   Q46QZ9_CUPPJ            Unreviewed;       626 AA.
AC   Q46QZ9;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   SubName: Full=Histidine kinase, HAMP region:Bacterial chemotaxis sensory transducer {ECO:0000313|EMBL:AAZ64435.1};
GN   OrderedLocusNames=Reut_B5087 {ECO:0000313|EMBL:AAZ64435.1};
OS   Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS   (strain JMP 134)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198 {ECO:0000313|EMBL:AAZ64435.1};
RN   [1] {ECO:0000313|EMBL:AAZ64435.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMP134 {ECO:0000313|EMBL:AAZ64435.1};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M., Schmutz J.,
RA   Larimer F., Land M., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 2 of Ralstonia eutropha JMP134.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC       family. {ECO:0000256|ARBA:ARBA00029447}.
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DR   EMBL; CP000091; AAZ64435.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q46QZ9; -.
DR   STRING; 264198.Reut_B5087; -.
DR   KEGG; reu:Reut_B5087; -.
DR   eggNOG; COG0840; Bacteria.
DR   HOGENOM; CLU_000445_107_16_4; -.
DR   OrthoDB; 5441488at2; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR   CDD; cd19411; MCP2201-like_sensor; 1.
DR   CDD; cd11386; MCP_signal; 1.
DR   Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR   InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR024478; HlyB_4HB_MCP.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   InterPro; IPR047347; YvaQ-like_sensor.
DR   PANTHER; PTHR43531:SF14; METHYL-ACCEPTING CHEMOTAXIS PROTEIN I-RELATED; 1.
DR   PANTHER; PTHR43531; PROTEIN ICFG; 1.
DR   Pfam; PF12729; 4HB_MCP_1; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF00015; MCPsignal; 1.
DR   PRINTS; PR00260; CHEMTRNSDUCR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00283; MA; 1.
DR   SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR   PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR   PROSITE; PS50885; HAMP; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000313|EMBL:AAZ64435.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Transducer {ECO:0000256|PROSITE-ProRule:PRU00284};
KW   Transferase {ECO:0000313|EMBL:AAZ64435.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        15..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        195..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          216..268
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          273..502
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
FT   REGION          562..626
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        608..626
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   626 AA;  65735 MW;  5B1554CA7D735A98 CRC64;
     MAWLRNLGIG TRLSLAFMLV VLLLIGVAVF GVTSLAGMNA SLHLTVEGRL LKVIDLGHVK
     QDALEIGVIV RDAALTEDPA LVQQNTQRID GMRKEMGATL DALGKLIAAS GRPDLQKTFS
     DLTSAREAYN GQLDMVLRQL GAGEFAGARA ALVVTLPAAQ RPYFEKLDEI MDGGRNLALA
     AVKQADAGFV WTRNVLLGLT ALAVLLAVLM GTAITRSITG PARQALEAAE ALATGNLRHT
     FNVRSSDEMG RMLAALERAF RHLAALVHGI QQASGSIDGA TREIARGNTD LSQRTEQQAA
     SLEQTAASME QLTSTVRQNA DNARQANQLA VNASDVATEG GRVVRDVVQT MDSISKSSSQ
     VADITGVIES IAFQTNILAL NAAVEAARAG EQGRGFAVVA SEVRNLAQRS SAAAKEIAEL
     IGGSVRQVQD GARQAEQAGK TMDDIVGAVR RVTDIMGEIS AASTEQTSGI EQVSLAVTQM
     ESMTQQNAAL VEQAAAAAES LMQQAGGLVN EVGRFDVAQG SPATLALDAV VPPRQIDPAP
     LPPMANPAAL AAPRARAAAV PAATRPPVQR KPQSQAVLAK RAPAVPAKER PPVGRQRQEP
     VLKTALRRPT GATQTAMADS GDWETF
//