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Database: UniProt
Entry: K8A3T2_9ENTR
LinkDB: K8A3T2_9ENTR
Original site: K8A3T2_9ENTR 
ID   K8A3T2_9ENTR            Unreviewed;       602 AA.
AC   K8A3T2;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=Sensor protein {ECO:0000256|PIRNR:PIRNR003167};
DE            EC=2.7.13.3 {ECO:0000256|PIRNR:PIRNR003167};
GN   ORFNames=BN137_3627 {ECO:0000313|EMBL:CCJ74230.1};
OS   Cronobacter condimenti 1330.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Cronobacter.
OX   NCBI_TaxID=1073999 {ECO:0000313|EMBL:CCJ74230.1, ECO:0000313|Proteomes:UP000009340};
RN   [1] {ECO:0000313|EMBL:CCJ74230.1, ECO:0000313|Proteomes:UP000009340}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330 {ECO:0000313|EMBL:CCJ74230.1,
RC   ECO:0000313|Proteomes:UP000009340};
RX   PubMed=23166675; DOI=10.1371/journal.pone.0049455;
RA   Joseph S., Desai P., Ji Y., Cummings C.A., Shih R., Degoricija L., Rico A.,
RA   Brzoska P., Hamby S.E., Masood N., Hariri S., Sonbol H., Chuzhanova N.,
RA   McClelland M., Furtado M.R., Forsythe S.J.;
RT   "Comparative analysis of genome sequences covering the seven cronobacter
RT   species.";
RL   PLoS ONE 7:e49455-e49455(2012).
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}.
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:CCJ74230.1}.
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DR   EMBL; CAKW01000130; CCJ74230.1; -; Genomic_DNA.
DR   RefSeq; WP_007679554.1; NZ_CP012264.1.
DR   AlphaFoldDB; K8A3T2; -.
DR   STRING; 1073999.AFK62_10835; -.
DR   KEGG; ccon:AFK62_10835; -.
DR   PATRIC; fig|1073999.7.peg.2272; -.
DR   eggNOG; COG3850; Bacteria.
DR   OrthoDB; 9811306at2; -.
DR   Proteomes; UP000009340; 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: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; cd22900; NarX_sensor; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 1.20.5.1930; -; 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:SF51; NITRATE_NITRITE SENSOR PROTEIN NARX; 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; 1.
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   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        154..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          176..228
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          397..587
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   602 AA;  67259 MW;  0229300A90BCA2FD CRC64;
     MLKRLFSPLT LANQLAMIVL LLAGLGMGGM ALAGWLAQGV QGSAHAINKA GSLRMQSYRL
     LAAVPVAKAQ TAMFNDMERT AWSEELEQAA VRDGQQAALQ AIQRYWRDRL SPALRDARSP
     QEVNAQVAQF VAQIDALVSA FDSSTERRIA QVVMLQRGMA VLMGLLLLFT LLWLRRRLLR
     PWRQLLAIAH AVAHRDFSQR ASVSGRDEMA TLGRALNSMS AELAESYASL EQRVQEKTAG
     LEQKNQILSF LWEANRRLHS DVPLCERLAP VLTRLQSLTL LRDIALRVYE VDDEEHYQEF
     VWQPDERCDE IGCHLCPRQL PAETETGTTL KWRLGDSHTQ YGLLLATLPA GCHLSRDQQQ
     LIDTLMEQLT ATLALERQQE RKQQLLVMEE RAAIARELHD SIAQSLSCMK MQVSCLQMQG
     DALTEESRTL LGQIRNELNA SWRQLRELLT TFRLQLNEPG LKAALVASCQ EFSARLGFPV
     VLDYQLPPRR VPSHQAIHLV QIAREALNNA LKHAGASAIH VSVTLHQGQV RLCVADNGCG
     LPDNAGRTNH YGLIIMRDRA QSLRGDCQVR RRTEGGTEVV VTFIPDAPFS SVPALIEGEV
     HE
//
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