ID K8A237_9ENTR Unreviewed; 894 AA.
AC K8A237;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BN137_2995 {ECO:0000313|EMBL:CCJ73616.1};
OS Cronobacter condimenti 1330.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=1073999 {ECO:0000313|EMBL:CCJ73616.1, ECO:0000313|Proteomes:UP000009340};
RN [1] {ECO:0000313|EMBL:CCJ73616.1, ECO:0000313|Proteomes:UP000009340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330 {ECO:0000313|EMBL:CCJ73616.1,
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 -!- 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:CCJ73616.1}.
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DR EMBL; CAKW01000107; CCJ73616.1; -; Genomic_DNA.
DR RefSeq; WP_007676788.1; NZ_CP012264.1.
DR AlphaFoldDB; K8A237; -.
DR STRING; 1073999.AFK62_06035; -.
DR KEGG; ccon:AFK62_06035; -.
DR PATRIC; fig|1073999.7.peg.1238; -.
DR eggNOG; COG2205; Bacteria.
DR OrthoDB; 9806130at2; -.
DR Proteomes; UP000009340; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0034220; P:monoatomic ion transmembrane transport; IEA:UniProtKB-KW.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd01987; USP_OKCHK; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 1.20.120.620; Backbone structure of the membrane domain of e. Coli histidine kinase receptor kdpd; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR038318; KdpD_sf.
DR InterPro; IPR025201; KdpD_TM.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR003852; Sig_transdc_His_kinase_KdpD_N.
DR PANTHER; PTHR45569; SENSOR PROTEIN KDPD; 1.
DR PANTHER; PTHR45569:SF1; SENSOR PROTEIN KDPD; 1.
DR Pfam; PF13493; DUF4118; 1.
DR Pfam; PF13492; GAF_3; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF02702; KdpD; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ion channel {ECO:0000313|EMBL:CCJ73616.1};
KW Ion transport {ECO:0000313|EMBL:CCJ73616.1};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CCJ73616.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000313|EMBL:CCJ73616.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 399..419
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 425..443
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 448..465
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 477..498
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 670..884
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 894 AA; 99088 MW; 084640CE807D4F47 CRC64;
MTEEPMRPDP DRLLVQTQGR TRGKLKIFFG ACAGVGKTYA MLQEAQRLRA QGLDILVGVV
ETHGRQETAA LLQGLAIQPL KRIHHRGRVV QEFDLDAALA RNPALILMDE LAHSNAPGSR
HPKRWQDVDE LLDAGIDVFT TVNVQHLESL NDVVGGVTGI QVRETVPDPI FDAADEIVLV
DLPPDDLRQR LHEGKVYIGG QAERAIEHFF RKGNLIALRE LALRRTADRV DDQMRAWRDR
QGQEKVWHTR DAILLCIGQG SGNEKLVRTA ARLAARLGSV WHAVYVETPR LHRLSETARR
AILSALQLAQ ELGAETATLA DPVEEKAVLR YAREHNLGKI VIGRRNKRRW WSQDTFAERL
ARQAPDLDLL IVALDDKPAP AAAKPADNRT FMEKWRVQLR GCAVALLLCA LITLVARQWL
IAFDAANLVM IYLLGVVVVA LFYGRWPSVL ATVINVVSFD LFFIAPRGTL AVSDVQYLLT
FAVMLTVGLI IGNLTAGVRY QARIARYREQ RTRHLYEMSK ALAVGRTARD IAATSQQFIT
STFHARGLLL LPDEDGTLQP PQPLAEMAPW DEAIARWSFD KGLPAGAGTD TLPGVPYQIL
PLRTAGKTLG LVIVEPSNLR QLMIPEQQRL LETFTLLVAS ALERLFLTES EEQARLVSER
EQLRNSLLAA LSHDLRTPLT VLFGQAEILT LDLASEGSKH APQASEIRQH VLNTARLVNN
LLDMARIQSG GFNLRKEWLT LEEVVGSALK MLEPGPGGRH IELQLHDPLT LIHVDGPLFE
RVLINLLENA AKYAGARAKI GVQTGWRDDR LDLEVWDNGP GIPAGQEQAI FAKFARGNKE
SAIPGVGLGL AICQAIVEVH GGEIYARNRP EGGASFHVLL PKETPPELDI HEVM
//
