ID Q3SSN4_NITWN Unreviewed; 766 AA.
AC Q3SSN4;
DT 11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT 11-OCT-2005, sequence version 1.
DT 24-JAN-2024, entry version 136.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Nwi_1446 {ECO:0000313|EMBL:ABA04707.1};
OS Nitrobacter winogradskyi (strain ATCC 25391 / DSM 10237 / CIP 104748 /
OS NCIMB 11846 / Nb-255).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Nitrobacter.
OX NCBI_TaxID=323098 {ECO:0000313|EMBL:ABA04707.1, ECO:0000313|Proteomes:UP000002531};
RN [1] {ECO:0000313|EMBL:ABA04707.1, ECO:0000313|Proteomes:UP000002531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25391 / DSM 10237 / CIP 104748 / NCIMB 11846 / Nb-255
RC {ECO:0000313|Proteomes:UP000002531};
RX PubMed=16517654; DOI=10.1128/AEM.72.3.2050-2063.2006;
RA Starkenburg S.R., Chain P.S., Sayavedra-Soto L.A., Hauser L., Land M.L.,
RA Larimer F.W., Malfatti S.A., Klotz M.G., Bottomley P.J., Arp D.J.,
RA Hickey W.J.;
RT "Genome sequence of the chemolithoautotrophic nitrite-oxidizing bacterium
RT Nitrobacter winogradskyi Nb-255.";
RL Appl. Environ. Microbiol. 72:2050-2063(2006).
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; CP000115; ABA04707.1; -; Genomic_DNA.
DR RefSeq; WP_011314715.1; NC_007406.1.
DR AlphaFoldDB; Q3SSN4; -.
DR STRING; 323098.Nwi_1446; -.
DR KEGG; nwi:Nwi_1446; -.
DR eggNOG; COG5000; Bacteria.
DR HOGENOM; CLU_019564_1_0_5; -.
DR OMA; IAWGEVA; -.
DR OrthoDB; 9776727at2; -.
DR Proteomes; UP000002531; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR003660; HAMP_dom.
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; IPR017232; NtrY.
DR InterPro; IPR045671; NtrY-like_N.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF19312; NtrY_N; 1.
DR Pfam; PF00989; PAS; 1.
DR PIRSF; PIRSF037532; STHK_NtrY; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ABA04707.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002531};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABA04707.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 26..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 99..124
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 297..322
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 323..376
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 388..460
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 513..735
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 738..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 766 AA; 83662 MW; F78A596BBB038AE7 CRC64;
MTTADTPVPS HDPTFAESRG WAMRRLLAPV AIGLALLSAF LTFVVLVGLT PIEPTHRVVI
TFLLVDAGII LLLVGIIARE VWRVVQARRR GRAAAKLHVQ VVGLFSIIAV LPAVVVSVVA
SVTIDRGLDR LFSGPIKEVI ENSRIVAHAY ANEHAQLIRG DILGMANDVS NARPLYDQDR
VTFLQLLTSS AKARNLPGAM LIDKEGHLLV SAQTGIKRAY DTPNPDILKN VNEDDPQIAL
IPEANYVAAV IRLRAFQDTF LYVARLLDPY VVSQLKQTES SIVEYATIEA RRLGIQVALA
LMFAVIALTI LMASVLLGLN FADRFVAPVR RLMNAANLVS TGDLNVQVPV LKSEGDLAQL
GETFNKMTAE LRTQRDELVN ASGLIDSRRR FIEAVLSSAS AGIIGVDGAN TIRILNRSAE
KLIGHSESET LGHPLSEVIP ELSDLMQTAR EGAQRLVQGQ ITLNRDGNER NISVRVSAEQ
TSQSRDSYII TLDDITELVT AQRTSAWGDV ARRIAHEIKN PLTPIQLSAE RIRRKFGKVI
TQDKPIFEQC TDTIVRQVED IRRMVDEFSR FARMPKPVME GEDVADTVRQ TVFLMRVGHP
EIDIEADIRQ EPMRAQFDRR LISQALTNII KNAAEAIEAV PPEVLGKGRI DVIAAQEEDD
IIIDVIDNGV GLPKVARARL LEPYVTTREK GTGLGLAIVG RVLEDHGGKL ELNDASAIRP
EARGAWMRLR FAATGPANAG TIGDDGATNG DTLTGKETKT EVATGG
//