ID G3IVG7_METTV Unreviewed; 1759 AA.
AC G3IVG7;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Mettu_1727 {ECO:0000313|EMBL:EGW22894.1};
OS Methylobacter tundripaludum (strain ATCC BAA-1195 / DSM 17260 / SV96).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylobacter.
OX NCBI_TaxID=697282 {ECO:0000313|EMBL:EGW22894.1, ECO:0000313|Proteomes:UP000004664};
RN [1] {ECO:0000313|EMBL:EGW22894.1, ECO:0000313|Proteomes:UP000004664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1195 / DSM 17260 / SV96
RC {ECO:0000313|Proteomes:UP000004664};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Held B.,
RA Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N.,
RA Ovchinnikova G., Pagani I., Klotz M.G., Dispirito A.A., Murrell J.C.,
RA Dunfield P., Kalyuzhnaya M.G., Svenning M., Trotsenko Y.A., Stein L.Y.,
RA Woyke T.;
RT "Genomic sequence of Methylobacter tundripaludum SV96.";
RL Submitted (JUN-2011) 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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; JH109152; EGW22894.1; -; Genomic_DNA.
DR STRING; 697282.Mettu_1727; -.
DR eggNOG; COG0457; Bacteria.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG3437; Bacteria.
DR HOGENOM; CLU_239136_0_0_6; -.
DR Proteomes; UP000004664; Unassembled WGS sequence.
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; 6.
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; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 6.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR NCBIfam; TIGR00229; sensory_box; 5.
DR PANTHER; PTHR43047:SF79; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 5.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF13424; TPR_12; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 5.
DR SMART; SM00091; PAS; 6.
DR SMART; SM00448; REC; 1.
DR SMART; SM00028; TPR; 5.
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); 6.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 5.
DR PROSITE; PS50112; PAS; 5.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:EGW22894.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000004664};
KW Transferase {ECO:0000313|EMBL:EGW22894.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 462..482
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 501..571
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 626..698
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 701..753
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 754..824
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 827..880
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 881..957
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 961..1014
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1018..1081
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1084..1134
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1226..1278
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1296..1513
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1536..1652
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 484..511
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1585
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1759 AA; 197334 MW; 0CCBBFD7ED8E2B57 CRC64;
MATVGNSYRS HALRGNAVQD APASRNAGAL LTEFPRRSVG TIVILIFALC GLAHADNALE
QWRSKAGEIR MLAENDTQRA YAEAERLQAD FPAYASPADR ARLLNLLARI EIYQAQTEKA
AAHIQHAMEL AKQHNDPVGQ AEADLNTTLN AINQARVDDA IAASIHGLAV LDGVDRPDLL
GEALLRMAMM YRRTDQLDES ITMSMQSLDI ARQSNNPLAL VYAYHGLAIA YELSDHFSEA
GEYYQRMLEQ ARIAGSRLME AYALLGLGYT HNNRGDLKSA EPLIREAVAV FHAIDVPFSV
NFSQFALADN LRKQQRYAET LPIFDEVIER YQRYPNKIGL WWVLNARSTH QMALGHIADA
HRDVEQAYKL AKEIGVPLYL TDSAKRLAEI AAAKGDYRQA YRFMFDASDT AAKAAKDTAA
TRMLQLTRRY QTESKQREID KLNRRNQQQA AELKHRTLEQ RWLWTVLGGS VIMLTGAAFF
LVRLRRSHRR LEALNTQVLQ AKNKLQATLD TIPDLLFEIG LDGRYYDYHS PCTELLLVPA
EDLLGKTVSD VMPAEAAKIV MSALREAHDQ GISTGKQFQL PLPHGDFWFE LSVAIKPTLD
KEEAHLIVLS RNITERKHME AQVLQREQEF RVLVENSPDL IFRYDKECRR IYTNPAVARL
VGRRADALLN MSPSEAKILS AGEADKLMQM IRQVQATGRP AESEVECLGA DGQLHYFHNR
YAPEFNAHGE VVGVISIARD VTERKQAAEA LAASEREFRT LAESLPDNIV RYDLEGRVIY
VNPVLEKTLG TIVSKMLGTT VRERFPNGEY DDYAQLLDAV LTSGEIGEIE KIVTPPYSNL
HLVHSIRMIA ECDENGEVIG VLAIGRDITE RKLAEQALRE SEEKYRTLIQ KIQAAVVVHG
ADTQILTFNL VAQEILGLSE DQLYGKTAID PVWHFFHENG CAASPDEYPV NKVLASGKAL
KNYVLGVHRP GRQQDVWVLV NADPVFGKDG KITQVIITFI DITQRKQAEQ RLWLVDFALN
QVREAVYIIN LQDHRFLNVN AEASRALGYS TEELLDLTIY DIDPDADSEG MENLQREIDA
GSLSVFERRH KTKDGRIFPV EINAQVFEYE GRPTSIALVR DITERKRVED EVRALNADLE
LRVLERTEAL RLQTRYLRTL IDTLPMLAWL KDKESRFLVV NQTMALACTL SVDEMVGKSD
LDCWPREYAE SYRAVDSEVM ATGRRKTVEG PFFDAHDGVI WVETFKAPVL DVDGSVLGTV
GIALDISDRR ALEMAREAAL AEAERLARLR SEFMARMSHE LRTPLNGILG YAQILLGESR
GNERQSAMLN VIQQSGEYLL NLINDILDFA KIEAGKQELS LSDIQLPSFL RNLASIITIK
AEQKALVFVC DIAADVPAGI RADETRLRQV LLNLLSNAIK YSERGQISLK VTVLEPGRLR
FEVQDSGLGI DTGQLDTIFQ AFEQAGDWQH RTGGTGLGLP ISRELVRMMD SDIHVTSRVD
EGSTFWFDLD VTVVEVCDDI MVAEQHIVGY QGLRRRVLVV DDANENRTLL IDILGRLGFE
TFEAANGRAC LDSVEAQTPD LILLDMVMPE MDGLETTRRL RCMQGFGQTP IIAVSASASG
SDVTEAMKAG VNVFLSKPID IKRLMVQIAV LLKLDWIYAL PEADAPLRQR LNEALVVPPL
EEMAILHRLA QEGSMRDIIL QTTYLEGLDQ SYRPFAAQLR ALAQDYQSKA ILDLVEGYID
SIVTTQRSQW NADAKSRRL
//
