ID A0A1I5NE66_9PSED Unreviewed; 793 AA.
AC A0A1I5NE66;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, 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 ORFNames=SAMN05216190_106116 {ECO:0000313|EMBL:SFP19982.1};
OS Pseudomonas borbori.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=289003 {ECO:0000313|EMBL:SFP19982.1, ECO:0000313|Proteomes:UP000198784};
RN [1] {ECO:0000313|Proteomes:UP000198784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17834 {ECO:0000313|Proteomes:UP000198784};
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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; FOWX01000006; SFP19982.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5NE66; -.
DR STRING; 289003.SAMN05216190_106116; -.
DR OrthoDB; 9797243at2; -.
DR Proteomes; UP000198784; 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 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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF79; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 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; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:SFP19982.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:SFP19982.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 187..208
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 215..232
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 252..271
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 283..305
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 338..361
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 428..646
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 672..788
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 721
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 793 AA; 87566 MW; AE0B24F1ED59774F CRC64;
MRYLLILLFA VWPLCASAVV FDEHTRMLPL GQAMQVFEDV RGDATIDEVT SSALQAGFRR
HDSPVLNAGY SRSVFWLRLD LEYRPQRPQR PDGPQPWLLE LAYPPLDRLD LYLADGQGKF
QLAQRTGDSL PFASRQIRHH NYLFELDLQP HQPQRVYLRL QSQGSIQAPL SLWAPTAYLE
EQPARSYVLG VIYGVLLVML IYNLFIFLSV RDASYLYYIL YIASFGLYQV SVNGAGIEYF
WPNNPWWANA STPFLIGSAA LFGCQFARSF LHTAEHSPWV DRTLLLLMAS GAGVMILALT
VSYALSLRLA TYLALLFTVV VFAAGIIAWL RGMRVARYFI IAWSAFLLGG AINSLMVLGY
LPNVFLTMYA SQIGSALEVG LLSLALADRI NAMKEERTRI LQDSGHKLEV LNQQLANSNR
LKDEFLASVT HELRTPMNGV IGSLELMQTL DLDAELAQYQ KTAAGSARDM MRMVDDILVL
SELQAGKLYP RREPFSLRGL LDGLRAQYAA RAADKGLRFV LELDESLPDT LAGDAGKLAQ
SLGYLLDNAI KFTGRGEIRL RVGATADGLL LSIEVIDTGV GFSVSQETSL YQHFHQLDGS
MTREYGGLGI GLAICRQLVD LQGGSLSHES QPGQGSRFRV QVPLILPSAL AAPPVPAPRA
PAQLARSPEQ CTVLVVEDNA INQLVTRGML LKLGYRVLTA DNGAEALEVL RREPVDAVLL
DCQMPVLDGF ATCRALRILP GCAELPVLAI TAHSHSGDRE RCLAAGMSDY LAKPVKFEAV
RGLLHDWVLC RAG
//
