ID G9ZVQ9_9PROT Unreviewed; 763 AA.
AC G9ZVQ9;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Nitrogen regulation protein {ECO:0000256|PIRNR:PIRNR037532};
DE EC=2.7.13.3 {ECO:0000256|PIRNR:PIRNR037532};
GN ORFNames=HMPREF9946_00625 {ECO:0000313|EMBL:EHM02935.1};
OS Acetobacteraceae bacterium AT-5844.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae.
OX NCBI_TaxID=1054213 {ECO:0000313|EMBL:EHM02935.1, ECO:0000313|Proteomes:UP000003292};
RN [1] {ECO:0000313|EMBL:EHM02935.1, ECO:0000313|Proteomes:UP000003292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AT-5844 {ECO:0000313|Proteomes:UP000003292};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (SEP-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 ECO:0000256|PIRNR:PIRNR037532};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|PIRNR:PIRNR037532};
CC Multi-pass membrane protein {ECO:0000256|PIRNR:PIRNR037532}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHM02935.1}.
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DR EMBL; AGEZ01000022; EHM02935.1; -; Genomic_DNA.
DR AlphaFoldDB; G9ZVQ9; -.
DR STRING; 1054213.HMPREF9946_00625; -.
DR PATRIC; fig|1054213.3.peg.590; -.
DR eggNOG; COG5000; Bacteria.
DR HOGENOM; CLU_019564_1_0_5; -.
DR OrthoDB; 9776727at2; -.
DR BioCyc; ABAC1054213:G1H32-594-MONOMER; -.
DR Proteomes; UP000003292; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-UniRule.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00082; HisKA; 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; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
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 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.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PIRNR:PIRNR037532};
KW Cell membrane {ECO:0000256|PIRNR:PIRNR037532};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR037532};
KW Membrane {ECO:0000256|PIRNR:PIRNR037532, ECO:0000256|SAM:Phobius};
KW Nitrogen fixation {ECO:0000256|PIRNR:PIRNR037532};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR037532};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000003292};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR037532};
KW Transmembrane {ECO:0000256|PIRNR:PIRNR037532, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|PIRNR:PIRNR037532}.
FT TRANSMEM 20..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 56..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 101..127
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 298..323
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 324..377
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 514..744
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 763 AA; 82868 MW; 4697389540A0F158 CRC64;
MSRAPAARPQ RAGRALADFL LGRFVTLALA VGALLMGIGT FTLLSNGSPF GPTKPGQVVA
MVLANALFLL LLLGSVIGRL VRVWAERRRG SAGSRLHVRL VLLFSATAVA PALLVAIFAA
VFFNLGIQSW FSDRVRSTLE ASLVASRAYL DEHRNNIRAD ALAIAADLNR NSTMLVDNQY
GFARLLATHT ALRGLTESIV FEPTLNQVVA HAGLTTTTVL DPLPAWAMEQ ARNGDVAVLP
SENEDARVRA LVALDIQPGL MLLIGRPVDP GVMEHMRYTE LSFQEYDQLD RNRSGLQITF
ALIFAIAALL VLLAAVSIGL VIANQIARPL SRLIVAADRV RGGDLTVRVT EGAADDEVGT
LSRAFNRMTN QLAAQRSELM EAYRQIDERR RFTETVLSGV SAGVVGLDAE GRINLPNRSA
SELLGHDLNG DLGTRFSEVV PEFAPLLEQA MAAPERSRVA EIRIGPPESR RTLMAQIGAE
MQRGQVAGYV LTFDDITELL SAQRKAAWSD VARRIAHEIK NPLTPIQLSA ERLKRRYLKQ
IQTDPETFVA CTDTIVRQVE DIGRMVDEFS AFARMPQPVI RPENPAQVAR EALVLHQNAH
HDIVFSTSIP DSLPRILCDR RLMGQALTNL LANAADAVHA RQQAEEAEAG AATPGHIRIS
VEPGEDSLAI AVEDDGVGLP QGEERERLTE PYVTHKPKGT GLGLAIVKKI MEDHGGRIVL
TDRRSAEDES ARGTRAVLIF PLRNAEGGEG TAAKMTEVQQ HGA
//
