ID V4P6F6_9CAUL Unreviewed; 898 AA.
AC V4P6F6;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AEAC466_16270 {ECO:0000313|EMBL:ESQ82694.1};
OS Asticcacaulis sp. AC466.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=1282362 {ECO:0000313|EMBL:ESQ82694.1, ECO:0000313|Proteomes:UP000017826};
RN [1] {ECO:0000313|EMBL:ESQ82694.1, ECO:0000313|Proteomes:UP000017826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AC466 {ECO:0000313|EMBL:ESQ82694.1,
RC ECO:0000313|Proteomes:UP000017826};
RX PubMed=24463524; DOI=10.1038/nature12900;
RA Jiang C., Brown P.J., Ducret A., Brun Y.V.;
RT "Sequential evolution of bacterial morphology by co-option of a
RT developmental regulator.";
RL Nature 506:489-493(2014).
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:ESQ82694.1}.
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DR EMBL; AWGE01000017; ESQ82694.1; -; Genomic_DNA.
DR RefSeq; WP_023459242.1; NZ_AWGE01000017.1.
DR AlphaFoldDB; V4P6F6; -.
DR STRING; 1282362.AEAC466_16270; -.
DR PATRIC; fig|1282362.3.peg.3216; -.
DR eggNOG; COG2205; Bacteria.
DR OrthoDB; 9806130at2; -.
DR Proteomes; UP000017826; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
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 Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000017826};
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};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 404..423
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 435..460
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 480..502
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 674..891
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 898 AA; 99159 MW; D0F3BE925B3CF4E7 CRC64;
MSPDTRPDPD KLLALVRHDG GEGVPRRGRL KVFFGASAGV GKTYAMLSEA RLRLRDGVDV
VSGVIEHHGR RETQALMEGI PVLPMLEIDH RGIRLTEFDL DGVLARRPGL VLVDEFAHTN
APGSRHPKRW QDVEELLDNG IDVYTTLNVQ HLESVNDQVA RLTGVWVRET VPDTIFEAAD
DIALVDIPSD ELLKRLADGK VYVAEGANTR AAENFFKKSN LLVLREMALR RTAERVDAQS
DELNAAMGQN EAQLGHKIML LIGPDPLSTR LIRHAKRMAA RGRAPWFAVY LQSDRHETLN
EKSRARVEQY LRLAENLGAQ VVRLSGAQPA RDILTYARQN GFTRIMVGHR RIRWWLKPFR
TAFAQQLIEN SDGIEISVIN GDVAPYSVTE NVASSLRPFI ARPIDYGVAS AAVALATLAG
LPFRDKTPSD NLTMLYLTAV VIVAARLGLG PSVVASILSV PAFNFFFAEP YYTFNFYDSY
YYITFVFMLV TSLVVGSLTA RLSRHARQVS ERERETQILY GLTRALSSVR GVDRICEVAI
SHLSAPYNLA VSLFVDSPEG LGCIPKSAGP EDMKEMSAVR WVATNTQMAG RDTDTLPSAS
GLYLPLQAEN ETLGVMGLTP NGNGRRFTGS EILQFETFAS LVAGALQRAR RSDEAERSKV
ESENERLRNV LLSSLSHDLR TPLTVMNGSV SLLLKMRKEL PRKAMDELTG LWGQLIRLQK
FVGNLLNMAA ITSGKMTLNF QPYMIQEIIG AALSQVQSTK ENRQLRTQIV GNLPMVQIDG
GLVEQVFVNL LENAFQHTAS DGEIVITAER DADRLRIRIS DNGAGLKTGD EARIFEQFQT
AQTLSSDRAG GTGLGLAICR GIVQAHGGMI YARNNSDKTG ASFIFTLPIV PEMPKEIL
//
