ID B8KTG4_9GAMM Unreviewed; 1947 AA.
AC B8KTG4;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=NOR51B_1736 {ECO:0000313|EMBL:EED35789.1};
OS Luminiphilus syltensis NOR5-1B.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC Luminiphilus.
OX NCBI_TaxID=565045 {ECO:0000313|EMBL:EED35789.1, ECO:0000313|Proteomes:UP000004699};
RN [1] {ECO:0000313|Proteomes:UP000004699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NOR51-B {ECO:0000313|Proteomes:UP000004699};
RX PubMed=23705883;
RA Spring S., Riedel T., Sproer C., Yan S., Harder J., Fuchs B.M.;
RT "Taxonomy and evolution of bacteriochlorophyll a-containing members of the
RT OM60/NOR5 clade of marine gammaproteobacteria: description of Luminiphilus
RT syltensis gen. nov., sp. nov., reclassification of Haliea rubra as
RT Pseudohaliea rubra gen. nov., comb. nov., and emendation of Chromatocurvus
RT halotolerans.";
RL BMC Microbiol. 13:118-118(2013).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS999411; EED35789.1; -; Genomic_DNA.
DR STRING; 565045.NOR51B_1736; -.
DR eggNOG; COG0642; Bacteria.
DR eggNOG; COG0834; Bacteria.
DR eggNOG; COG4251; Bacteria.
DR HOGENOM; CLU_234848_0_0_6; -.
DR OrthoDB; 9810730at2; -.
DR Proteomes; UP000004699; 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; cd00088; HPT; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd01007; PBP2_BvgS_HisK_like; 2.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 4.
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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
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 InterPro; IPR001638; Solute-binding_3/MltF_N.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 2.
DR Pfam; PF00497; SBP_bac_3; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00062; PBPb; 2.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 2.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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:UP000004699};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..1947
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002876200"
FT TRANSMEM 685..702
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 723..741
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1224..1445
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1464..1585
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1613..1729
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1769..1870
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 1517
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1662
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1808
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1947 AA; 213805 MW; 67DE68C211EDB6C8 CRC64;
MMESRVSRGE RRNLLAALLL LAVTISCAAF AQDRTEGGRS ENYVVRLVQL VQTIELQNEV
LYGSASQYVY TGDTFWLDRY RSATENFDAA LGELERDYQS SDQLAMRRLL EAADSLHGIE
SRAFDDYDAG RLEEAQALMS SREYRRNWDK LSSAVDTLRE TAEHLIESGL VLDMNWQPLV
LTEKERRWIE ENPVIRVGRE MDWAPHLFID DQGRVKGTIV DVLDALRRKT GLEFQLTDPV
RNPILKRKLV DGDIDLIPAV TQVSSRLQGR LLTSHYMNLE IAAYVLAESP LNGVNQLYDK
RIALPENAPK DGLILDAFPD LNVVSVKSVA VALDRLEAGE VDGILATKSA VLKEADRRGL
QNLRELGTGN SLMPIRMAVR QEQPILRDIL SKAISSLTNG ERKTIMSRWV DAETLAASSS
TLKLSPEESA WLRNHPGMLL GRDANWPPFE FVNNRGEYTG IVAEYARAAS SALGVRFNPV
RGLSWEDVLK RAQRKEVDIF AGLTRTAERE SYLLFSKPYL SMPTAVLTLD DAPDLLRVSD
LGDQSIGVVG GYAVEEWARD RYPEANFVAV ASVAEGLKKV ARKELGAMLA NQYSAAYIVD
ELNLENIRVN FRTEYSYQLA MGVRNDWPEL IPILNRLIDN ISPAARAEYR ARWIGADVAE
STDTLSGQGS GSLDESSLLP RLENILLAIG LILIFMGGFW WLSGRGGDIQ KLYQSGRLRY
LTLFAVIGVV AFTFLAAQYA LTRQERIVRA RAADTLATVA RAASESMQRW ARAEMRLVSR
LANEPFLETV FTMHSSAQNG FVEGVEKQRV LSDLIPSRED ASRLTVLLRD GTSVFDSDPG
LSHLMPELRQ TVFAGNTTFI PPRRLTDETG ASRSEMYFAA PIIDHAGRPI AAVVATVDPG
AEFTSSLGNA VVGQSGETYA FDQSGLMLSN SRFSEQLAEL GRLPKGGSTV AYLRLTDPGG
DLTEGFTPNR SPSRWPTTAM FQAALQRETG AIPDGARDYR GRRVLSAWVW VPELDIGIAA
EIDESEALDS YVLAENILYA VLGISLTLAL SLLGLTTWVA SRANKALLLA RDELEDKVEA
RTEELSESRY LFQTVLDNSP AAISVKDLDS RYLLVNKIWR QVMSLTRSGV VGFTTRELLP
AELAERSEQE DSAVVESGDV IQGQARIKNA EGEVRVFLSY KFPVFDAKGE CFAVGSVLSD
VTELNHAMEI ADDANQAKSD FLANMSHEIR TPMNAIIGMS HLALQTDLTS KQRNYIEKVH
RSAESLLGII NDILDFSKIE AGKLDIEAVD FRLDDVMDNL VSLVGLKAED HGLELLLDVP
PDLPTALIGD PLRLSQILIN LGNNAVKFTE DGEVVVAVRV EEESNAEVRM HFSVRDSGIG
MNKEQQSRLF QSFSQADSST TRKYGGTGLG LAISKQLVAM MDGEIWVESE PGVGSDFQFT
ACFEKQQGEI PEPTVAPDDL GPLPILVVDD NQSAREILAA ILESLGFQIK TASGGRQAVE
MIKAADADEP FKLVMLDWRM PGLDGVQTGQ LIQEDTTLKN QPKIIMITAF GREEMQEGAG
GLAISGFLTK PATASSLLDE IMRAMGREVA ENPRGGDRKQ AVKEFAAELR GAQVLLVEDN
EINQELAVEI LTTHGMTVQV ANNGQEALDL IAAHQFDGVL MDCQMPVMDG YEATRHIRNN
PATKDLPVLA MTANAMVGDK EKVIEAGMND HIAKPINLAD LFKTMAKWIS PANPVAEPEA
SAELPIEEEA LPELPGIDTN RGLGTTGGNM KLYRRLLGKF RDGNVNFEKE FSAALDAGDQ
DTATRLAHTL KGVSGNIGAL ELQAEAGKLE HACDAGEPNN ALREQLVFVQ SLLAQVLVGL
GPITAPEESA TANGSGRSPE EIKAILGRLR DLLENFDTEA SDVVEELSVE PSLVLHKPLL
KKVNAAMEEY DFDAALEYLD ALDTALA
//
