ID A0A1H7N555_9BURK Unreviewed; 1032 AA.
AC A0A1H7N555;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05216319_1218 {ECO:0000313|EMBL:SEL18439.1};
OS Duganella sp. CF402.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Duganella.
OX NCBI_TaxID=1855289 {ECO:0000313|EMBL:SEL18439.1, ECO:0000313|Proteomes:UP000198529};
RN [1] {ECO:0000313|Proteomes:UP000198529}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF402 {ECO:0000313|Proteomes:UP000198529};
RA Varghese N., Submissions S.;
RL Submitted (OCT-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; FOBG01000001; SEL18439.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7N555; -.
DR STRING; 1855289.SAMN05216319_1218; -.
DR Proteomes; UP000198529; 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; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.60.40.2380; -; 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 InterPro; IPR011623; 7TMR_DISM_rcpt_extracell_dom1.
DR InterPro; IPR011622; 7TMR_DISM_rcpt_extracell_dom2.
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; IPR036641; HPT_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; PF07695; 7TMR-DISM_7TM; 1.
DR Pfam; PF07696; 7TMR-DISMED2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000313|EMBL:SEL18439.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:SEL18439.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1032
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011474196"
FT TRANSMEM 188..206
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 215..236
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 280..302
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 308..328
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 416..637
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 683..799
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 852..952
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 732
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 891
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1032 AA; 111993 MW; B37125BDF1B0A064 CRC64;
MLRHLARFLL LILALAFIPS VALADAGPLV LRAQHDYAEA WPVVRVMADA DGRLTPEAAL
AAAEHYAVPN SAYATLGVHK DVMWLRIPVS VPAGSDGEWI LNIDYAVLNR VDVYVASGGR
ITQHRVTGNL QPDSDGAAPG RVPAVLLHLT PGADHVLLLR VQNVGAMILP ISLARPARFH
GAALNEQMLQ GVLTGLSLCL LMYSIAQWST LREPLYGKFA LLVLGTTLFS VEFFGLGNQY
LWNNSAWMSS HAGGVFALTA SCGAYLFVQE ALARNGKDKI FSRLMYGGAA LCVVSALCYA
TDFMSVETLV IVVSTLGVMP MLLGLPGAYF RARRGDAVGI YFLLGWGVSF ASSAVLSQVI
SGKVGANFWT MHALQFGNMF DMLVFTRILG LRTKAMQSAM LRAEEATRTK SEFLAHMSHE
IRTPMNAIIG MSRLALMTEP NPKLQNYLGK ILGAGEHLLA VINDILDFSK IEAGKLGLES
APFELREMLD HLASLTVIKS DAARVELKMR VDDSVPARLV GDPLRLSQVL INLTSNAVKF
TERGEINVAV ELMDKTADTV ALRFSVSDTG IGMRPSQVSN LFQSFHQAGA TTTRKYGGTG
LGLSISRQLV ELMGGDIQVF STPGIGSRFS FIVRLGIADE RTAPVDWPLH PHQQRPQQAA
REMRRSDNAG LAMRDLSALD GARILLVEDN ANNREVALDF LSVARMQIDV AEHGGEAVRM
VDQADYDLVL MDVQMREMDG LTATRRIRAM ERCQHLPIVA MTAYAMAGDR DKSLAAGMND
HITKPISPEQ LFRTLIKWIP PSRLAARRAQ ANAALYTAPT PADYSGVAAS SAPLPSIPGL
DWQLALEGVD RQRGRLDRRI RGFLQEYQPA AQAVREAIAS GHHEALHSLT HNLKSTAAYI
GAVHLAEQAQ ALEHALRNGR SDRIPMLATE LADGLDLVVG GLSQLNETPA PVRYRDGDAA
LLIARLEAFL RSDDARADDV LDELRALPLA VRHAGLLAAI AAAVDDIEYQ AALAPLSALA
RALQNETEEE RA
//
