ID A0A0A6PKT0_9GAMM Unreviewed; 469 AA.
AC A0A0A6PKT0;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=PN36_12865 {ECO:0000313|EMBL:KHD06434.1};
OS Candidatus Thiomargarita nelsonii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Thiomargarita.
OX NCBI_TaxID=1003181 {ECO:0000313|EMBL:KHD06434.1, ECO:0000313|Proteomes:UP000030428};
RN [1] {ECO:0000313|EMBL:KHD06434.1, ECO:0000313|Proteomes:UP000030428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hydrate Ridge {ECO:0000313|EMBL:KHD06434.1};
RX PubMed=27199933; DOI=10.3389/fmicb.2016.00603;
RA Flood B.E., Fliss P., Jones D.S., Dick G.J., Jain S., Kaster A.K.,
RA Winkel M., Mussmann M., Bailey J.;
RT "Single-Cell (Meta-)Genomics of a Dimorphic Candidatus Thiomargarita
RT nelsonii Reveals Genomic Plasticity.";
RL Front. Microbiol. 7:603-603(2016).
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:KHD06434.1}.
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DR EMBL; JSZA02000041; KHD06434.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A6PKT0; -.
DR Proteomes; UP000030428; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd19920; REC_PA4781-like; 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 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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 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; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000030428}.
FT DOMAIN 9..125
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 262..469
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 120..161
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 58
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 469 AA; 52631 MW; 79614A71BD1A26BC CRC64;
MEIQNSKNII LVVDDSRTYL VVLSQILKKQ GYKVETASNG KQALKSVQST LPDLILLDIQ
MPEMNGYEVC QKLKADDKTR EIPIIFISGL NKIIDKLKAF SLGGVDYISK PFKKEDVLAR
VETHLKLHRL QQQLAAQNQE LQKALEELRN TQEELIQAEK MAALGQLIAG VAHEINNPLS
AINSSVMTIN NFLTQTITQL PEFFRSLSEE KQQAFFALLQ TSLAKETLLS TKEERELKRK
LISQLKNIED ADIVADTLVD MGIYDNVEEF LSLLQAPDSE IILDFAYKLS NLQRSSKTIE
TASQRASKVV FALKKFARFD QSGQKVEANI TDGIETVLTL FHNKLKHDIE VIKHYAPLPP
ILCYPDELNQ VWTNLIQNAL QAMDYKGTLT IKVSQQDKQA FISMTDSGKG IAEEIKEKIF
EPFFTTKGAG EGSGLGLDIV RKIIEKHEGN IAVESQPGKT TFTVSIPIH
//
