ID A0A090AJI7_9GAMM Unreviewed; 2313 AA.
AC A0A090AJI7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, 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=THII_1395 {ECO:0000313|EMBL:BAP55692.1};
OS Thioploca ingrica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Thioploca.
OX NCBI_TaxID=40754 {ECO:0000313|EMBL:BAP55692.1, ECO:0000313|Proteomes:UP000031623};
RN [1] {ECO:0000313|EMBL:BAP55692.1, 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; BAP55692.1; -; Genomic_DNA.
DR STRING; 40754.THII_1395; -.
DR KEGG; tig:THII_1395; -.
DR HOGENOM; CLU_230039_0_0_6; -.
DR OrthoDB; 5605755at2; -.
DR Proteomes; UP000031623; Chromosome.
DR GO; GO:0016020; C:membrane; 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; cd00130; PAS; 7.
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; 3.30.450.350; CHASE domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 11.
DR InterPro; IPR006189; CHASE_dom.
DR InterPro; IPR042240; CHASE_sf.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 9.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF03924; CHASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 3.
DR Pfam; PF08448; PAS_4; 2.
DR Pfam; PF13426; PAS_9; 4.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM01079; CHASE; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 10.
DR SMART; SM00091; PAS; 11.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 11.
DR PROSITE; PS50839; CHASE; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 7.
DR PROSITE; PS50112; PAS; 7.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000031623};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 70..292
FT /note="CHASE"
FT /evidence="ECO:0000259|PROSITE:PS50839"
FT DOMAIN 517..589
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 593..645
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 646..716
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 720..772
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 845..900
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 994..1046
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1173..1243
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1247..1299
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1300..1372
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1376..1428
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1429..1471
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1556..1605
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1631..1682
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1707..1748
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1854..2070
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 2100..2216
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 336..402
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1673..1704
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1827..1854
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 2149
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2313 AA; 267918 MW; 0D931588033C3EC8 CRC64;
MRYKYKMTVL LLVIGSIFSI TGFITVRQLE QQKIYFEMTK LAPKQIWSLQ NALQNMVEML
HTLANFYAIN PDGLDRQQFN TVTTPILLRH PYLFTLIWAP RVPHNQRSHY ESMAQANYPQ
FRFTEHSSQE EFITASLRNE YFPIYYATSL NSIEHIYGFD LQSNYLFAQL LSQAKEKEIL
QATSRVKWIV DNSVDQDTIL VFYPIYQKKM AINTGAQQQK YLRGFLVTVI RLKSLVQQVL
EKSPHRDDFN LQIEDESASP NERLLYADSS SEKTLPAYQE PFEFAGRVWL ITAFPKVNDS
LLTQNWLSFS ILIGGLAITV LMSRYLYTIT QQTQQLQIEI AQRRRAEIAL QQAEESLIEY
NLTLEQQVSE RIQELAEKNS LLQQKIQERQ QAEQTLHDST RHFNTILDNL PAFICLYASD
RRIQFANRYF YEKIQPILTN FEQQLTAPAQ ASVEELAAAD VFEKGLLSKV WEQPLANNRT
YQIYEYPFVD SDGSVLILKM GIDITQHKQL EKALRASEER FELAMRGAND GLWDWNLETN
ELYLSPRWKS MLGYQDQELV NHFDEWSKRI HPDDLTHAIG DIEAYLDRKK PTYENTQRIC
HKNGHYVWIL DRGIAVWNKE GKPTRFIGIR TDITAQKQAE AALRNSQERI NRFFELPLIG
MAITSPTKGW LEVNDKLCEM LGYSREELKQ QTWSALTHPD DLAADSEQFN RLLSHQIEGY
SRDKRYIHKN GNLVYTTLSL RCVRSTQGEV DYLVVLIQDI TERKQAEKKL REQEEFLRLL
IDNIPQYVFW KDIHSVFLGC NRRFAYLIQV NNPAEIIGKT EFELLREPLA QWLHENDSYV
MSTNRALYHH LEEVIWSDGQ SRWFETNKIP LHDAQGKVIG ILGTSEDITE RRRVELVLRE
YNQTLEREVA ERTQALRKQD TFLRLVLDNI PQLISWKDIN LVFLGCNQRV AQFANLNSTD
DIIGKTDFDL IWRDYAEHFQ HQDRQVIETN TPIYHAIDQV LRSDGRLFWW EVNKIPLYDD
SGKVVGVLGT VEDITAHKQA EDALKQAHER FKIVLNSLNS AVYVSDMQTN EILFVNHSIQ
KLFAQELVGT ICWQTLQPVG QSAVCDFCTN SRLISTTGQP TGVCTWEYHN KRLNKWFYVQ
DCAIPWDDGH LVRLSVATDI TERKQTEDKL REREARLKAI FDNAATGIVL INMKGQIIQC
NTKWLEMTGY TPAAIGSLSY FSLIHLDDIK YQQNYYKQLI NKEIKSYQVE QRLLKNNGEL
FWVNVSVTAI YDSTEMLEAL VGIMVDITER KQVESALRQS EERFDLAMQG SNDGLWDWNL
DTDSVYFSPR WKQMIGFQEQ EMSNRFEELI NRIHPDDSSL VLAKIEDYLS KKTPVYEVQF
RLQHKEGHFI WILSRGIAVW NKQGIAYRFI GTHMDLTAQK QAEQALRESE IYWRNLIEGA
LIGLLLVDTQ GKIIEANPAY AHIVGYPLEE LYQLTIWDIT PKKYFSLEQK QLHLLKTTGR
FGPIEKEYIH KHNYLVPVRL SGLLVTRKGK HLIWCNVEDI TDQKQAKAKL QNAYRELARF
KTILDITLDS LFMFDDETYR FLYVNQGAIQ QFGYSAEELL QKTLLDLRTE LATERFETVV
NTLRNHSQPT TTFETTLQYK EGNQIPVEIF LQYIQIPGQV KCFVAIMRNI SERKQMEQAL
RQSKAELEIT VAQRTQELQE KQKLLEEQQK FTALVENSND VIGISTLEGQ VSYLNKAGRR
LVGLEQNQRP LEKTQLTDYL AESLRPLWQQ AIFPKVLQQE HWEGEVQLRH FQTGQLIETH
SNVFIVRHPH TGIPLCLATV TRDITEQKRA SIQLQQAKEA AEAANRAKST FLANMSHELR
TPLNGILGYT QILSRDRTLS NKHKQGIHII ERSGHYLLTL INDILDLSKI EAGKLELYPV
DFNFIHFIQS ITEIFQVRAQ QKGITFIYEP LSSLPMGIHA DDKRLRQILL NLLGNAIKFT
HQGQVKLQVG YDKNKVRFQV EDTGIGIAAA EIDKIFLPFQ QVGDPTYRIQ GTGLGLAITK
KLVELMGSEL QVDSVLGQGS LFRIELELPA VVGLETTEPL ESQALITGYR GRDELAKRYK
ILVIDDQLEN RLVIVNLLTP LGFEVIEAPH GQEGLDKVQT ESPNLIILDL IMPVMNGFEF
VQQLRQISKY KEMVVIATSA SVFNQYKEES LSAGCNEFIA KPIRAEILFN YLQRYLPLEW
IYESVPKNNL IAEHNDNKAL FSSIALPSQV ATQLFELTQM GDINGIIEQA QQLQQLDERF
APLAARIIRL AQQFEDEKIS ELVKPYLASK VEH
//
