ID K0C2W8_CYCSP Unreviewed; 771 AA.
AC K0C2W8;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=barA {ECO:0000313|EMBL:AFT66863.1};
GN OrderedLocusNames=Q91_0825 {ECO:0000313|EMBL:AFT66863.1};
OS Cycloclasticus sp. (strain P1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Cycloclasticus.
OX NCBI_TaxID=385025 {ECO:0000313|EMBL:AFT66863.1, ECO:0000313|Proteomes:UP000006282};
RN [1] {ECO:0000313|EMBL:AFT66863.1, ECO:0000313|Proteomes:UP000006282}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1 {ECO:0000313|EMBL:AFT66863.1,
RC ECO:0000313|Proteomes:UP000006282};
RX PubMed=23144416; DOI=10.1128/JB.01837-12;
RA Lai Q., Li W., Wang B., Yu Z., Shao Z.;
RT "Complete genome sequence of the pyrene-degrading bacterium Cycloclasticus
RT sp. strain P1.";
RL J. Bacteriol. 194:6677-6677(2012).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003230; AFT66863.1; -; Genomic_DNA.
DR AlphaFoldDB; K0C2W8; -.
DR SMR; K0C2W8; -.
DR STRING; 385025.Q91_0825; -.
DR KEGG; cyq:Q91_0825; -.
DR PATRIC; fig|385025.3.peg.841; -.
DR HOGENOM; CLU_000445_104_15_6; -.
DR Proteomes; UP000006282; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00088; HPT; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR036641; HPT_dom_sf.
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 PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 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; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000313|EMBL:AFT66863.1};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AFT66863.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000313|EMBL:AFT66863.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000006282};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 152..170
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 172..227
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 267..484
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 509..627
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 665..765
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 558
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 704
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 771 AA; 85664 MW; 8AD4408E7ECE60E9 CRC64;
MPAAIVAIIL ATYLTSTRLN DMYDLLHKTN ENLCLSIAKS SVNGVFSGNL AALDAVVRSV
VNEPDILSIK ITDSAGTALS YASSDIATPS LLSNPSKEIV QPITLKSIEN TDEFDSLLVG
LPVEKNETIG YVTLTLSYEA IQQRQYNILS NTIYITLFLL LVIALIAKYF SATISRPILK
LTRDVKNITK GNYTPPPNTP NISSKDEIAT LESGVHEMAQ QINNHQRILK QRVLEATQEL
RSQNDKLFSA QEEILKSADA KSRFISHISH EIRTPLNGII GFLEIIQQTP LDDEQLKLVN
ASHLSSKNLQ TIINEVLDFT QLESGKVLIH KTNFELKKAI QDAILLLSAQ AKENHVSINY
QHDANVPVVI NQDHVKFGQI LINLLSNAIK FSHQSSVIVR LKMNPYKQDV IDISIIDHGI
GISGHNLKQL FQEYSQLDGA TSDQGTGLGL VITKRLLNAL NGSIKVKSTL GEGSNFTFSL
PFTQVKDSYQ AINKPIAIEH PLPDLSSLNI LVADDNEINR LLLSHLLEKQ HANVTCVNDG
QQAIELAFKH PYDLMLFDLR MPLKMGNEAL FEIRNHSQNP NYKTPAIAIT AHITSGEEKA
HHISSFDGYL IKPINQVHFF ALIEQLLSEH DFDTQPFIST TTNGDSASNS QPFDYHLAKK
SMNADHSFML IMLEKFLSEL PKQSEDISEL IGQNNIVDAA EAVHKIHGSA AYCGTPLLKS
AAKKLELVLR ENDKNNTQKF HKIFCNEIQT LLTLKSDILT LLQTLTNNQE T
//
