ID G7ZCH4_AZOL4 Unreviewed; 542 AA.
AC G7ZCH4;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=AZOLI_p20210 {ECO:0000313|EMBL:CBS89377.1};
OS Azospirillum lipoferum (strain 4B).
OG Plasmid AZO_p2 {ECO:0000313|EMBL:CBS89377.1,
OG ECO:0000313|Proteomes:UP000005667}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=862719 {ECO:0000313|EMBL:CBS89377.1, ECO:0000313|Proteomes:UP000005667};
RN [1] {ECO:0000313|Proteomes:UP000005667}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4B {ECO:0000313|Proteomes:UP000005667};
RC PLASMID=Plasmid AZO_p2 {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; FQ311870; CBS89377.1; -; Genomic_DNA.
DR AlphaFoldDB; G7ZCH4; -.
DR KEGG; ali:AZOLI_p20210; -.
DR HOGENOM; CLU_000445_133_5_5; -.
DR OrthoDB; 7325042at2; -.
DR Proteomes; UP000005667; Plasmid AZO_p2.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd06225; HAMP; 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; IPR005467; His_kinase_dom.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
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 Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CBS89377.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Plasmid {ECO:0000313|EMBL:CBS89377.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CBS89377.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 22..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 163..185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 186..239
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 291..525
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 542 AA; 57439 MW; 4A71F54B403936EC CRC64;
MLRGCLTRFG AVFSESLMVR TVGLICLPLL LAVGLAVVVA ISFSNRDART ALEARARQTV
ALLAGGVGDA LWNVDRVAAQ SILHPLSKDP DFVGAVVFER GGSVFLGLGE VDPPRSGLIV
EQVSLIRLTA GGQAGEQGRG QHIGQLRLYL TTANAERTIN SRAWAIALSG LGLLVAVCGL
LAVIVRGVTA PVRQMTDGMA VLAAGRIDLE IPRVDRRDEI GRMAAALGTL KQHAAERLEF
IERQARHMEV IEEIVAKRTG ELTAALETLK LAQNELIRSE KLAALGGMVA AIAHEINTPI
GSSLTVATTL SDKITEFQAI LQGKELRRSV IRDYSDSFGT ASQLLVGNLL RASELIGRFK
RVAVDQTGEL RRRFELDVVC GEVVAMLRPT YRHSPVSIDL RLPGGVVMDS FPGALGQVLT
NLMTNAMLHA FADATAAGSI TVGATLEEDG RHVTLTVADD GAGIPAAVLP RIFDPFFTTK
LGSGGSGLGL HIVYAIVMRV LGGVVAVESQ IGQGTRFSIV LPLVAPQQSG QDAVEEPVIM
PS
//
