ID A0A1W6E0Q2_9BACT Unreviewed; 1233 AA.
AC A0A1W6E0Q2;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=A6C57_00865 {ECO:0000313|EMBL:ARK08976.1};
OS Fibrella sp. ES10-3-2-2.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Fibrella.
OX NCBI_TaxID=1834519 {ECO:0000313|EMBL:ARK08976.1, ECO:0000313|Proteomes:UP000193660};
RN [1] {ECO:0000313|Proteomes:UP000193660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ES10-3-2-2 {ECO:0000313|Proteomes:UP000193660};
RA Kim M.K., Srinivasan S., Kim E.B., Kim K.S.;
RL Submitted (APR-2016) 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; CP015317; ARK08976.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W6E0Q2; -.
DR STRING; 1834519.A6C57_00865; -.
DR KEGG; fib:A6C57_00865; -.
DR OrthoDB; 9811889at2; -.
DR Proteomes; UP000193660; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00088; HPT; 1.
DR CDD; cd00130; PAS; 4.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 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 Gene3D; 3.30.450.20; PAS domain; 4.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
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; 3.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF6; RESPONSE REGULATORY DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00989; PAS; 2.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 4.
DR SMART; SM00091; PAS; 4.
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; SSF55781; GAF 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 SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ARK08976.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000193660};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 5..76
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 80..132
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 133..203
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 499..552
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 553..607
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 624..676
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 694..915
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 943..1065
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1141..1233
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 657..684
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 998
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1180
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1233 AA; 137525 MW; 7AA3F262EFED65EC CRC64;
MITTQPFDVR KTVDQLNLIG LTVEHDGSVS YVNPYALRVT AWSIDEIVGR NFFDVLVPPD
DRLVLEQVFR EALERGGFPE QREIQLLTKS GSTRNVHLNS FIPSGTGGRT DAFTIIGEDL
TSKRRVASAL SNTNAQLQDL VDNTSDLIQL ITLDGKFIFV NKAWRELLGY GADQIASLTL
NDVLHPDYVK STIDRLQRVQ EGEPNPSFET VFRSRDGRTL FLSGSVNCRY DQGKPTAFRC
ILRDITQKIR AEKAQRLYYS IASWTLNMPN LDDFYQRVHR ELGNIIDASN FFIALYDQSK
KYLTFPYYVD ESFQGNMRFT KKRLGSGLTE YTIQANKPLF LRDTDILHLA DEHHIDLYGQ
QQPKLMLTAP LRIGDEITGI IGVKSYNDPN LYGPRDLELL EFISGQVALA IARKQAEAAL
NKQTARLNAI FNSSTYLIWS VNKALQLTSF NQNYASLIQQ LTDEQPRLFI SAEKQGWRGV
GDDNQRLLDD RYKLAFKGQP QNFEMRFDLA GKESWLELHL NPILLTGGVI EEVSGIARDI
TNRKGAQLNL ERSEEKFRGI FENLQDIYVR VDRHGQITMV SPSVFKRSGY TPDEVMGQSA
LTYFVDPGVV RRALFKLVRT RSVRNFEATL RRKDGSERQF MFNMLLLKDE DGRYSVIAAL
ARDITELKRQ SAELVKAKDE AERSLKVKER FLANMSHEIR TPMNGVIGMV DLLNDTVLND
EQRDYVRTIR RSSETLLNIL NDILDLSKIE AGKMVLHEAP VALGEVFEKL IALFGQQANA
KRNRLFYTLS PDLPKYVIAD QTRMLQILSN LTSNALKFTE DGTVEVAAAL VSKRGKFNRI
KVEVRDSGIG ISAENIGLLF NSFSQVDTSS RKTFGGTGLG LSISKELAAL MKGEVGVEST
VGMGSTFWFT LELKETAISP TQSQSEAAAD MKVADFFTDY HPVILLVDDN AVNRKVASEI
LRKSGCVVTT ASSGPEAIEK VAAGSGLGDN RFDVIFMDIQ MPDMDGVETT RYLRDQYAAL
LPPVVAMTAY SMREDRERFL SQGLDDYIAK PIRAQGLISK VAEILKKTGR GQVRTTEVSS
LPTPETIASP APSPEQRTQL AVALPNGQPA SAIFDASLLL LYADVPVIDN DILEQLRDIG
GAELVESVFD DFVTEATELV TESLTAFAAG DIATVKSHLH TLKGSAGTVG VARLARIARE
AEGKLKVQDT SQLAQELKAL EAAFAEFMAT PQP
//
