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Database: UniProt
Entry: A8ADC1_CITK8
LinkDB: A8ADC1_CITK8
Original site: A8ADC1_CITK8 
ID   A8ADC1_CITK8            Unreviewed;       566 AA.
AC   A8ADC1;
DT   23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   23-OCT-2007, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   RecName: Full=Sensor protein {ECO:0000256|PIRNR:PIRNR003167};
DE            EC=2.7.13.3 {ECO:0000256|PIRNR:PIRNR003167};
GN   OrderedLocusNames=CKO_00321 {ECO:0000313|EMBL:ABV11484.1};
OS   Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=290338 {ECO:0000313|EMBL:ABV11484.1, ECO:0000313|Proteomes:UP000008148};
RN   [1] {ECO:0000313|EMBL:ABV11484.1, ECO:0000313|Proteomes:UP000008148}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696
RC   {ECO:0000313|Proteomes:UP000008148};
RG   The Citrobacter koseri Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (AUG-2007) 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:PIRNR003167};
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; CP000822; ABV11484.1; -; Genomic_DNA.
DR   RefSeq; WP_012131314.1; NC_009792.1.
DR   AlphaFoldDB; A8ADC1; -.
DR   STRING; 290338.CKO_00321; -.
DR   GeneID; 45134594; -.
DR   KEGG; cko:CKO_00321; -.
DR   HOGENOM; CLU_000445_20_10_6; -.
DR   OrthoDB; 9811306at2; -.
DR   Proteomes; UP000008148; Chromosome.
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:UniProtKB-UniRule.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:UniProtKB-UniRule.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd16917; HATPase_UhpB-NarQ-NarX-like; 1.
DR   CDD; cd22899; NarQ_sensor; 1.
DR   Gene3D; 1.20.5.1930; -; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 1.20.120.960; Histidine kinase NarX, sensor domain; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal 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; IPR029095; NarX-like_N.
DR   InterPro; IPR042295; NarX-like_N_sf.
DR   InterPro; IPR016380; Sig_transdc_His_kin_NarX/NarQ.
DR   InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR   PANTHER; PTHR24421; NITRATE/NITRITE SENSOR PROTEIN NARX-RELATED; 1.
DR   PANTHER; PTHR24421:SF66; NITRATE_NITRITE SENSOR PROTEIN NARQ; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF07730; HisKA_3; 1.
DR   Pfam; PF13675; PilJ; 1.
DR   PIRSF; PIRSF003167; STHK_NarX/NarQ; 2.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF158472; HAMP domain-like; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR003167};
KW   Cell inner membrane {ECO:0000256|PIRNR:PIRNR003167};
KW   Cell membrane {ECO:0000256|PIRNR:PIRNR003167};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR003167};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR003167};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR003167};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008148};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR003167};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012,
KW   ECO:0000256|PIRNR:PIRNR003167}.
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        147..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          174..227
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          364..559
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   566 AA;  63436 MW;  59DAC632225E1528 CRC64;
     MVVKRPVSAS LARAFFYIVL LSILSTGIAL LTLASSLRDA EAINVAGSLR MQSYRLGYDL
     QSGSSQLNAH RQLFQQALNS PALSNLNAWY VPQTVKSRYG QLHANWLEMN TRLVDADIKW
     YRANINNYVD QIDLFVLALQ HYAERKVMLV VGISLAGGIG IFTLVFFTLR RIRQQVVQPL
     NQLVAASQHI EHGQFDIPPL NTHLPNELGL LAKTFSQMSS ELHKLYRSLE ASVEEKTHDL
     HEANRRLEVL YQCSQALNTS QIDVHCFRHI LQIVREHDAA YYLELTVGDN WRISEGAESA
     DLPMQILPVT MQETVYGELH WQSPNVSAST PLLHSVSTML GRGLYFNQAQ KHFQQLLLME
     ERATIARELH DSLAQVLSYL RIQLTLLKRS IPEDNLPAQS IMADFSRALN DAYRQLRELL
     TTFRLTLQQA DLPSALHEML DTLQSQTSAK LTLDCRLPTL ALDAQMQVHL LQIVREAVLN
     AIKHASATEI AVSCVTAPDG NHTVYIRDNG VGIGEPNEPT GHYGLNIMRE RAERLSGTLN
     FSQPSGGGTL VSISFRSSED EEGQLA
//
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