ID A0A090AHM4_9GAMM Unreviewed; 1989 AA.
AC A0A090AHM4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=THII_0500 {ECO:0000313|EMBL:BAP54797.1};
OS Thioploca ingrica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Thioploca.
OX NCBI_TaxID=40754 {ECO:0000313|EMBL:BAP54797.1, ECO:0000313|Proteomes:UP000031623};
RN [1] {ECO:0000313|EMBL:BAP54797.1, ECO:0000313|Proteomes:UP000031623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kojima H., Ogura Y., Yamamoto N., Togashi T., Mori H., Watanabe T.,
RA Nemoto F., Kurokawa K., Hayashi T., Fukui M.;
RT "Ecophysiology of Thioploca ingrica as revealed by the complete genome
RT sequence supplemented with proteomic evidence.";
RL ISME J. 0:0-0(2014).
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};
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DR EMBL; AP014633; BAP54797.1; -; Genomic_DNA.
DR STRING; 40754.THII_0500; -.
DR KEGG; tig:THII_0500; -.
DR HOGENOM; CLU_000445_34_0_6; -.
DR OrthoDB; 9801841at2; -.
DR Proteomes; UP000031623; Chromosome.
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; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR CDD; cd14014; STKc_PknB_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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR041664; AAA_16.
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; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43642; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE G; 1.
DR PANTHER; PTHR43642:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE G; 1.
DR Pfam; PF13191; AAA_16; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00069; Pkinase; 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; 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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000031623};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..266
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1526..1755
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1781..1897
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 1485..1519
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1830
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1989 AA; 225030 MW; 2048D9887314BD4E CRC64;
MKLPHHPTFT CIYESANTLV YRLFKHQAKK PLIFKVLRKD YPTVEELKRY QHEYKILRHL
NAIGIIKAYG LKKYQNTLVL ILEDFGGESL KQWLAITPLT INQFLPIALQ ITESLEQIHV
AQVIHKDINP SNIIINRETK QLKIIDFNIS TYFPIRNPAG VNPNPLEGTL AYISPEQTGR
INQLVDYRTD LYSLGITFYE LLTGQVPFDY PDPLELIHCH LAKIPTPLHQ INPAIPPIIA
NIIMKLMAKN VEQRYQSAAG VKADLAKCLQ QLESFGTLDR FQFDLASDDF SAQFEIPQRF
YGREPEQQAL LHAFERTVQG NSELLLIAGY PGVGKSALVH EMSQAITEKR GHFISGKFQQ
YQQNVPYSAV SATFNQFCHD LLSENLEQLT YWRQTLLSAV GNNGQILIEV IPALEAIIGK
QPAVAQIKPI QTQNRFNLVF QRLVRSLAQA SHPLVLFIDD WQWADVASLE LLSNLMTDKE
SHYLLIIAAY RDNEINASHP LMITVEKLQI AQVIINTILV SNFSIAEVNA LIADTLKSAP
TSTLRLTQVV YDKTQGNAFF TQVFLTALYE QGLLHFNWQT RHWQWDIDKI TAQDFTDNVV
ALLVDKITRL PPDTQTVLKL AACIGNPFKL QTLSWIYYPD ELLTTFVHLW KAIAMGLISV
VQGSLPVSRY RDHELLQSEF KFQHDRVQQA AYSLMTDTDK LSIHLQIGRW LRANTPITAL
DSTLFEIVNH LNKGQKLITD PAEQIQLAQL NLLAGRKAQL STAYQHAVDY FRVGIALLEP
QGWEMQYELT LALSLAAAEV AYLSGRFDQM ESLITVVWQQ AKTLLDKIKV YEIKIQANMV
QNQPQAAIRI ARQALKWLGI NLPTKPSQLT IQLNLMTTRL RLIGKSIADL TELPEVTDAR
IRAMMRLLSM SLSAAYFHAP ELLPIIVLKL VNLSIKYGNI QESTCGYAIY GLILGGIAED
FERGLQFGQL AVNLIERFQA KSLKTSLAAV LVSIKCWKNH MKETLDPLRV AYQNGLENGN
LEYAGYTALQ YLLYSFCTGQ DLAKLEQEII SLNKIMTQVK QATALHYQKL FLQIILVLRD
NTENSRFFSD ELTDEQSPQL FQLANDKIIM FLLHFNKLVL CYLFGKYQQA VYYAIFLENY
LDHIIDTPHF SLFRFYDSLV HLAIYGEVSK SEQWRILKKV TANQQKISKW AYHAPMNFLH
KFYLVEAEYY RVRGQNAKAM DLYDRAITLA KENQYLHEEA LASELAAQFY LAQDKAKIAE
IYLRDAHYSY SQWGAKAKVA DLEMKYAPFF EKRTFSATAS SVTTTITSTS HLANTLDLAS
VLKASQTLAS EINLKQLLDK LMTIVIENAG AQRGLLIKES VAGETQWLVE AVGTIDKAGT
VELQTVEPPA TISFPITLIN SIAHTKTSIV LPDAQYKMRF IHDPYIVKHQ VKSMLGIPLL
NQGRLIRILY LENALIANAF TPARLAVLNL LSSQLAISIE NSSLYNQLEQ KVAERTDELQ
QEILERQRAE KSAQVANQAK TIFLANMSHE LRSPLNTILG FTQLMTLNSN LSVEQRENLD
IIHRSGEHLF TLINDILDLA KIEAGRATLN ETRFNLQQLL SEVEKTFQLR ANDKQLQLWF
KLQPNLPHYV QTDELKLRQV LINLLNNAIK FTPVGSIIVR VGSNILDNSL SRVEKKLTSQ
ICFEIKDSGI GMSDEELDTL FKTFVQTQAG IKTKEGAGLG LAISQKLVQL MGGEIEVSSE
IGKGTLFKFS ITVQELEESH LANSTVTRRV IALEPGQPHY RILIVDDNKF NRQLLVKRLN
PLGFELQEAM NGLEALEIVP RFQPHLIWMD LQMPVMDGYE ATKRIKASTQ GATTVIIAIT
ASVLEKEQAQ ALAAGCDDFV GKPFQEKAIF DMMNKYLGVR YVYKESDIIT KPPSVITLTP
ATLANLPTDW KKAVNAAAER ADAALILKLV AQIQDEHADL AKSIVALVEN FEFEQLISLT
NLSSTEEQP
//
