ID C1ACS7_GEMAT Unreviewed; 741 AA.
AC C1ACS7;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=GAU_3262 {ECO:0000313|EMBL:BAH40304.1};
OS Gemmatimonas aurantiaca (strain T-27 / DSM 14586 / JCM 11422 / NBRC
OS 100505).
OC Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC Gemmatimonadaceae; Gemmatimonas.
OX NCBI_TaxID=379066 {ECO:0000313|EMBL:BAH40304.1, ECO:0000313|Proteomes:UP000002209};
RN [1] {ECO:0000313|Proteomes:UP000002209}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T-27 / DSM 14586 / JCM 11422 / NBRC 100505
RC {ECO:0000313|Proteomes:UP000002209};
RA Takasaki K., Ichikawa N., Miura H., Matsushita S., Watanabe Y., Oguchi A.,
RA Ankai A., Yashiro I., Takahashi M., Terui Y., Fukui S., Yokoyama H.,
RA Tanikawa S., Hanada S., Kamagata Y., Fujita N.;
RT "Complete genome sequence of Gemmatimonas aurantiaca T-27 that represents a
RT novel phylum Gemmatimonadetes.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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; AP009153; BAH40304.1; -; Genomic_DNA.
DR RefSeq; WP_015895073.1; NC_012489.1.
DR AlphaFoldDB; C1ACS7; -.
DR STRING; 379066.GAU_3262; -.
DR KEGG; gau:GAU_3262; -.
DR eggNOG; COG2204; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_421965_0_0_0; -.
DR OrthoDB; 5416228at2; -.
DR Proteomes; UP000002209; 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 CDD; cd00156; REC; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003660; HAMP_dom.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000002209};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 298..350
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 370..594
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 615..731
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 666
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 741 AA; 80794 MW; E2EBD82740CE44E6 CRC64;
MRRRPISIAL KFPLLITGIV LTTSALLVWA TYQHFSAVLH DSAEARLRSS GVLLASSLAD
SYTAARAQLL AVANHPHVRE HLSTGQNVRG VDSILAVALA TTDSARLQIR VLDLAGREHR
IAKASHEAVG APWAVDTSMH EAFSSGGIRV SPLLDVGGVV EYEMIAPVHT RDDGESHVGY
IVETRRIRAQ GVDAVRGIVG TSAMLMGQPG SSVWTDFQRV VREPAVMVRP DSIARLVGTD
GRPAISIAER IGGSPWVVWL EYEEDRILAP LRSFVERMIP ITVLVALLGA LFAWAFSRKI
ANRLVVITRQ FDDVNAHQPS GAVREAGRDE IHLLEESFLA MSQRAERQAQ LESQLMQSQK
LEAVGRLAGG IAHDFNNMLT VVRNYAEMVR SELEPESPMS KDMDEILHAT SHAAQLIRQL
LAFSRQQILQ PVRLDLNDVI RNAHRMLQRV LPSHVEFRLD LGHPISTVLA DPGQIEQVLM
NLTVNASDAM PQGGRLTFRT TMSELDDTTE PAAAGVVGAR RYVCLTVVDT GIGMDHATTA
RIFEPFFTTK PVGKGTGLGL AGVHGIIAQL GGSIWVYSQP GRGTTFKVYL PAAEGAADPV
PRAGGGSPLI HDSGTILLVE DDPSTRGVIR RLLERHGFDV VEAANGVEAI AQLDDVHERV
RLVLSDVMMP ELNGMALANI IAERWPTMPV MLMSGYTDAD IPQQNSGALK RTFIEKPFTS
GALLHAVMRE LYTTEDVLKP R
//
