ID A0A399ER71_9DEIN Unreviewed; 1103 AA.
AC A0A399ER71;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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:RIH86063.1};
GN ORFNames=Mrose_01951 {ECO:0000313|EMBL:RIH86063.1};
OS Calidithermus roseus.
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Calidithermus.
OX NCBI_TaxID=1644118 {ECO:0000313|EMBL:RIH86063.1, ECO:0000313|Proteomes:UP000265341};
RN [1] {ECO:0000313|EMBL:RIH86063.1, ECO:0000313|Proteomes:UP000265341}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 110900 {ECO:0000313|EMBL:RIH86063.1,
RC ECO:0000313|Proteomes:UP000265341};
RA Da Costa M.S., Albuquerque L., Raposo P., Froufe H.J.C., Barroso C.S.,
RA Egas C.;
RT "Meiothermus roseus NBRC 110900 genome sequencing project.";
RL Submitted (AUG-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RIH86063.1}.
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DR EMBL; QWLA01000034; RIH86063.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A399ER71; -.
DR OrthoDB; 5389090at2; -.
DR Proteomes; UP000265341; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; 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; cd00088; HPT; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 2.
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; 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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_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; PF13185; GAF_2; 2.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 2.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00091; PAS; 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; SSF55781; GAF domain-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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:RIH86063.1};
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:UP000265341};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RIH86063.1}.
FT DOMAIN 473..696
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 716..831
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 859..975
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1006..1099
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 766
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 908
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1045
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1103 AA; 121912 MW; 5EFF7922427DD55F CRC64;
MPDPRDTRLQ SARYAMLSEV VLAIAQTTDL SSLLEQVIRR VKWVLDFERC TLALANDDGE
TYCLQTLLEV RRSVAPRNCE WVPLGQDLPG AVIESRQLRV LTDLFTQREK YTPWVDPALW
DGSLKSALSL PLEAYGKVLG ALTFATSKPE AYGDEDRKVA RTVATHLALA IDHLRQTEKL
AWLASFPQLN PGPVFEVDLQ GNILYLNPAA ESILPESPQD RARHPFLAEL PAIEATLRQS
GQISAVREVQ AGERWYHQMF RHVPGREGRL RFYVVDITER RRYQERLQRQ NELLAALQQT
TVGLLRRLEL SELLQDIVSR AGELLWTPHG FVTLLEPAGY LEQRVGTGVF AATIGLRFAP
GEGVSGQVWV RGQPLVVSDF GSWDYRNPSF DYSQICSAAV VPLHSGEQVV GTLGVAYGRD
SAREFEEEDI ELLTRLASLA SLALDNARLF AEMQRAKDAA LSANEAKSAF LATMSHEIRT
PMNAIIGMTG LMLDTALTPE QREYAETVRN SSESLLTIIN DILDFSKIEA EKLELEHQPF
DLRECVEGAL ELLSAKAAEK GLELAYLIAP STPEAIVGDV TRLRQILVNL LSNAIKFTEQ
GEVVVTLEGT PLEEGGYELH FAVRDTGMGI PPERMDRLFR SFSQLDASTT RRYGGTGLGL
AISKRLAEMM GGRMWAESAG IAGQGSTFHF TLRAEAAPRA ARAFLQEGHP ELQGRRVLIV
DDNATNRRIL EQQAESWGMP YRATASPREA LAWVEQGEPF DVAILDMQMP EIDGLTLARE
LRRLRDEKAL PLVMLTSLGR RELGEAEGLF QVFLTKPIRP SQLFNALVGV FAAQPRPLPQ
TERGPSSFDP QMGQSFPLRI LLVEDNATNQ KLALRLLERM GYRADVAGNG LEALQALERQ
TYDLVLMDVQ MPEMDGLEAT RHIRQRWPQA PLFITAMTAN AMEGDRELCL AAGMDDYLSK
PIRPEALAGV LGRASAHLRL EAPASAAEVE LDPAALEELR ALAGGDSAFL SELVETFLKD
GLALIQSLQQ ALEADNAAGV RMAAHTLKSG SAQFGVRGLA ELCKELEERG KAGLLEGAGA
LLERVRLEFE RVRPSLQALR EGG
//
