ID A0A074TM07_9RHOB Unreviewed; 770 AA.
AC A0A074TM07;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DL1_19790 {ECO:0000313|EMBL:KEP70028.1};
OS Thioclava dalianensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Thioclava.
OX NCBI_TaxID=1185766 {ECO:0000313|EMBL:KEP70028.1, ECO:0000313|Proteomes:UP000027725};
RN [1] {ECO:0000313|EMBL:KEP70028.1, ECO:0000313|Proteomes:UP000027725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DLFJ1-1 {ECO:0000313|EMBL:KEP70028.1,
RC ECO:0000313|Proteomes:UP000027725};
RA Lai Q., Shao Z.;
RT "The draft genome sequence of Thioclava dalianensis DLFJ1-1.";
RL Submitted (MAR-2014) 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};
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:KEP70028.1}.
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DR EMBL; JHEH01000008; KEP70028.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074TM07; -.
DR STRING; 1185766.SAMN05216224_106214; -.
DR eggNOG; COG4191; Bacteria.
DR Proteomes; UP000027725; 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; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 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; IPR011006; CheY-like_superfamily.
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; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
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; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 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 SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:KEP70028.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000027725};
KW Transferase {ECO:0000313|EMBL:KEP70028.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 45..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 402..625
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 653..769
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 704
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 770 AA; 83689 MW; C6F730E4B556FF7A CRC64;
MAQIELTLQP MTRTMAWLAP GAIYLAFAGV LAAGIAILVP DRVLMWALFS ASGTLLVVAA
ATWFAFAYHR TRRTRLHDLI SQFIAQDASP SFTTDSDGEI GFQNRAAVER FGSRGGQVLS
RALSELFADP AAVLRRLQLK AQALGAARED LVTRRGHVRL SVHQVGAEGY LWRLEDMAER
AIGGHGAETI SLPMLTVSES GTILFLNEAM RRLIGERVRT LDRVFRDLPL RSGEMHEVAT
PAGPVRATIA QIEGPGGRSE IYLLPISAEQ AQPQVGSFEI LPIALMKLDT QGRVAAVNRA
ARGLMGKTTE GAHLSDLLEG LGRPVSDWVA DALDGRADRR PEVLRARRGD KEVFLQVTLA
RIFEEGRAGL LAVLSDATQL KTLEAQFVQS QKMQAIGQLA GGVAHDFNNL LTAIAGHCDL
LMLRHDKGDP DFADLDQISQ NTNRAASLVG QLLAFSRKQT LKPQMIDLRD TVSEMTHLLN
RLVGEKVSLT LSHDPELRPI RADKRQLEQV LMNLVVNARD AMPGGGEITI TTENLHLVQD
IPRDRVTVPK GDYVAIQVSD QGTGIAPEVT RKIFEPFFTT KRTGEGTGLG LSTAYGIIKQ
TGGYIFCDSV VGSGTCFTIY LPAFDRVIDV DADEPEPARE LPVTREASSK PATVLLVEDE
APVRAFASRA LKLQGFNVLE AENAEEALAM LEAPDLAVDI FVTDVIMPGL DGPSWVAQAR
ESRPGIKTIF MSGYAEDVFK NGDSPIDNSV FLPKPFSLSE LTATVQNQLG
//
