ID C1A7I2_GEMAT Unreviewed; 1389 AA.
AC C1A7I2;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 77.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=GAU_1150 {ECO:0000313|EMBL:BAH38192.1};
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:BAH38192.1, 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; BAH38192.1; -; Genomic_DNA.
DR RefSeq; WP_012682639.1; NC_012489.1.
DR STRING; 379066.GAU_1150; -.
DR KEGG; gau:GAU_1150; -.
DR eggNOG; COG5000; Bacteria.
DR HOGENOM; CLU_258471_0_0_0; -.
DR OrthoDB; 9781147at2; -.
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 Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS 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; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR000014; PAS.
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; PF02518; HATPase_c; 1.
DR Pfam; PF13188; PAS_8; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 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 Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:BAH38192.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW 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 TRANSMEM 38..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 63..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 288..306
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 318..341
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 353..376
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 383..403
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 423..441
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 453..474
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 480..498
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 505..523
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 742..763
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 784..807
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 963..1015
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1138..1376
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 1389 AA; 147404 MW; 392CA73142A96594 CRC64;
MRPRLPVATP SDRWPVAWVS ASAGALVALA YWQQDPGWLR LAAAVAVTAW AAWLVPTVRQ
PRTVAVLSVA AIATGLLIAS SDTATLVALR SNWAGWSAAE RESRAQRVAA SVTDVAGVLR
DLTRQLAADS TLMAEVSTGR IRSLSAPLPR GVESALLVYH RGDLVARAGQ AHTEFPASDV
PGVRLIDGAF HTSLVARDRS PDGQMEVVAL ALVSSAPPAD RFARPLLQTL PGGFDVAHTV
VESPDSVHVE LGTTVVVVPD GARRLARVRA TTFTEGETRL RFEQRARMRT SVALAIAMVG
ILVVAWRRPA GTPERMAAAI AVLAGVSMAP LTGLSNVSPL FDPASYFAPM GGSLTATIAA
LLITAALVLA VLLFALRTRD GRYSRLLSGG LVIALAFGGP FLLRDLARGI ALPAAGAGFG
LWVSWQLALA LVGAAILLAG ASAGRAVLGG RRGLPPVVTL LIAAIAGGLA PALWEAPGTW
PAWYPALWIL AIVTLALTRR GLSQIMAAAV VAGAGAATLT WGATVRARLA LAQHDLERLA
VVDDNALRLL ERFATTLRDE TRPVQRSDAL LRRYAASELA LAGYPARLAR WSAEHPDSAV
SVLELAPVND TLGAQAYLAQ LARQSGALEL RFVDDGPTTL LMAAVPAIDG TVTTIAVPPR
TRLLPTDPFA AYTGVTGSRG SAPPYRLEFS GVTAGDSVPR ALSWRRRGEA MHGDGVAGGA
SGVRGVHVEV DLRGLDALVP RGALLVLLDV GVVMLLWSAT ALADGALGRW LRVRRVRWSR
SYRVRLSGAL LMFFIAPAAI FALWAWYRLQ DDDRAARELL LRETLRVAST EQEQRMLGTA
PSSTGAPLFL YHRGMLTTAS DSLLDALAPL GRLSPVTFVD DAAASEEVFT TRRIAAGPIS
ALVGYRRLGR SDDAARAESM LATPARGDEF ALDARREDLG VLVLFATMLG ALAAVWSSGI
AARALARPVG VLREAALAVA AGRDAPMLGA APATEFAPVY RAFGRMAEDL ATSRAALEAA
QQRTAAVLQH VASGVLAIVA NGDIILANPR AEAMLGVALP AGRASLWQLP RLFDDLVARA
RRFLASDAEE DAFDLALPAR QLRARLTRLP TGAVLTLDDV TELASAQRVL AWGEMARQIA
HEIKNPLTPI RLGVQHLRRA FRDGRSDFGQ ILDTNVGRVL AEIDHLDEIA RAFSKYGTAP
EDRMPAVSVD VVEVVHDVIA LEQLGDEERR DTVHWLVERD TTLAEGDTVA FALRDELREV
MINLLENARL AGARTVTVRV SPASAPGGYD HETPHLPRLA DERSHGLAIE VTDDGVGIAP
ETLPRVFEPH FSTRTSGSGL GLAISRRLIE GWGGAIGLTS EPGVGTAVRI VLRRAPEGAE
AGRTLPRYS
//
