ID A0A1V3NUX6_9GAMM Unreviewed; 939 AA.
AC A0A1V3NUX6;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=B1C78_00010 {ECO:0000313|EMBL:OOG28774.1};
OS Thioalkalivibrio denitrificans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thioalkalivibrio.
OX NCBI_TaxID=108003 {ECO:0000313|EMBL:OOG28774.1, ECO:0000313|Proteomes:UP000189462};
RN [1] {ECO:0000313|EMBL:OOG28774.1, ECO:0000313|Proteomes:UP000189462}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ALJD {ECO:0000313|EMBL:OOG28774.1,
RC ECO:0000313|Proteomes:UP000189462};
RA Ahn A.-C., Meier-Kolthoff J., Overmars L., Richter M., Woyke T.,
RA Sorokin D.Y., Muyzer G.;
RT "Genomic diversity within the haloalkaliphilic genus Thioalkalivibrio.";
RL Submitted (FEB-2017) 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:OOG28774.1}.
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DR EMBL; MVBK01000001; OOG28774.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V3NUX6; -.
DR STRING; 108003.B1C78_00010; -.
DR OrthoDB; 6017161at2; -.
DR Proteomes; UP000189462; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 3.
DR CDD; cd00156; REC; 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; 3.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR014757; Tscrpt_reg_IclR_C.
DR NCBIfam; TIGR00229; sensory_box; 3.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 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; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 3.
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; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS51078; ICLR_ED; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:OOG28774.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000189462};
KW Transferase {ECO:0000313|EMBL:OOG28774.1}.
FT DOMAIN 1..167
FT /note="IclR-ED"
FT /evidence="ECO:0000259|PROSITE:PS51078"
FT DOMAIN 16..86
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 87..140
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 297..341
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 373..423
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 424..478
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 502..552
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 572..797
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 823..938
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 873
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 939 AA; 102907 MW; CCE27EC074BD04B7 CRC64;
MEVTDSRADG QTMAGREAPL QEILDNTTAV IFVKDREGRY LLVNRRFLEV VGRTAEQVLG
RPETEVVPRG VAERFRENDR RVFERGEPVE FEETYRLPDG EHSFLSLKFP LRDADGRIYA
VCGISTDITA RKRTEEALRK VAMDVSAAAG GDVLAEIACS VAETLGADVA MVGKRVGEEP
VRIQALAVCL RGERAGPVEY ALEGTPCAHV VGRSFLYIPD GIQSRFPGDS MFAELDMHSY
AGYPLFDSAG EPTGLIAVLH GSRLPDAEFI ESILRIFSVR AAAELERMAA EEVRRASELS
YRAIIEASED AIYIHDLDTG AIVDVNPKAC LALGYSRDEM LHLTVDQLSS GVPPYTGAEA
ARLIDRARHG ERPRFEWHRR NRDGSLHWDE VWLKRVNLGG VERIVAITRE ITERKEREEA
LRRSEDRLRA TVEASLDCII GMDTEGRITE FNPAAEQCFG HRRAEVMGRV LADLIIPERF
RASHHAGLAH FRATGEGPYL GKRVEVTAQR ADGSEFPAEL AIDVVRSGEE DLFIGYLRDI
TERHRAETAR TQLETQLRQA QKMEAIGHLT GGIAHDFNNI LTGVMGYVVL AQERAAAGGD
AKLLQYLERA SESAVRARDL IQQMLTFSRG QRGDPRPLDP VPLVKEAIKL LRSTLPATVS
LVTELNARVP AVRADPVQVE QVLMNLCINA RDAMGGRGAI HVRLRHRSGV HGVCASCREP
VQGDFVELSV GDEGPGIAPE HLDRIFDPFY TTKGPGQGSG MGLATVHGIA HEHGGHVELV
TAPGTGAEFR VLLPALAEVP DGRNEAAVGS RQGVEVASAL HGRVLLADDD PSAGAFMEEL
LRDWGLDVVR AFDGLEARRL LQTDGPFQLA LLDRAMPGLS GLEVAAWIRD HAPSVPVVLY
TGYSEDLAES ALDEAGVRAL LRKPVNIEAL RRVLEATLS
//
