ID G7Z3L1_AZOL4 Unreviewed; 685 AA.
AC G7Z3L1;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 68.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=AZOLI_0639 {ECO:0000313|EMBL:CBS86006.1};
OS Azospirillum lipoferum (strain 4B).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=862719 {ECO:0000313|EMBL:CBS86006.1, ECO:0000313|Proteomes:UP000005667};
RN [1] {ECO:0000313|Proteomes:UP000005667}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4B {ECO:0000313|Proteomes:UP000005667};
RX PubMed=22216014; DOI=10.1371/journal.pgen.1002430;
RA Wisniewski-Dye F., Borziak K., Khalsa-Moyers G., Alexandre G.,
RA Sukharnikov L.O., Wuichet K., Hurst G.B., McDonald W.H., Robertson J.S.,
RA Barbe V., Calteau A., Rouy Z., Mangenot S., Prigent-Combaret C.,
RA Normand P., Boyer M., Siguier P., Dessaux Y., Elmerich C., Condemine G.,
RA Krishnen G., Kennedy I., Paterson A.H., Gonzalez V., Mavingui P.,
RA Zhulin I.B.;
RT "Azospirillum genomes reveal transition of bacteria from aquatic to
RT terrestrial environments.";
RL PLoS Genet. 7:E1002430-E1002430(2011).
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};
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DR EMBL; FQ311868; CBS86006.1; -; Genomic_DNA.
DR AlphaFoldDB; G7Z3L1; -.
DR STRING; 862719.AZOLI_0639; -.
DR KEGG; ali:AZOLI_0639; -.
DR HOGENOM; CLU_401530_0_0_5; -.
DR OMA; ARERSMP; -.
DR Proteomes; UP000005667; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
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 InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR032255; HBM.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43047:SF5; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM01358; HBM; 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 PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CBS86006.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 308..327
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 329..382
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 414..642
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 363..404
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 685 AA; 73381 MW; FAECD40A4BE597B8 CRC64;
MKRNGILSRS GRRTRFRDMT VSARVGTGFA IALGLVVLLA LVGFGWFHAV SRDIGAFSGR
ADLSQAAADA DVSLRDLEVA VRDHLTYGDD QSLLDASWRH DTLRERLDTL SKGAVEIADR
QGVDKAKSAL DDYWAAVQKV IALRSDRNGQ ITGVLEPMVA QTRQKLDHLK SAGGVDSTAL
ASDAAIAVLL MQDHLTRFID RRDPQDAEAM RAQLAAARDR LAEMNRYLWV PGTKQAIDEV
AALLSKAGGV LTAIEAAVAE EDSLRAEAMA ANAAGIAANL GEIRRRAEAG TQALRSTLTD
GLSGYTKVAL WIGGAVLLAG LLALWLVQRS VAAPMKTMAT AVTALAAGRT DVTLPTLTGQ
DDIAAMARAV EVLRTTAEDT ERERREAEME HTRLLREKAL AETASRAKSD FLVNMGQELH
GPLTEIVNAS QSLMTDLHRL GVDELASDVE HIQWTGEQLT TLVDALLDYA KIEAGAMDVC
LQDFDINRLL TEARERSMPA ADLYGNALEL SAPAGLGQMH SDFTKVRQTL LNLLDNACKF
TQEGTVTLSA ERVERNGARW YRFIVTDTGR GFPSAQTGRL FQPFVQGAGN GTVATRGQGK
PRGAGLGLTL VGHYTAMLGG EIEVASEPGQ GTRITVALPA IYEAPAEERA LQVEAVGNAK
PLLRVASLKP AGHLAGSNSM TQIGP
//