ID A0A251XBT0_9GAMM Unreviewed; 896 AA.
AC A0A251XBT0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=TPSD3_00215 {ECO:0000313|EMBL:OUD16186.1};
OS Thioflexithrix psekupsensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thioflexithrix.
OX NCBI_TaxID=1570016 {ECO:0000313|EMBL:OUD16186.1, ECO:0000313|Proteomes:UP000194798};
RN [1] {ECO:0000313|EMBL:OUD16186.1, ECO:0000313|Proteomes:UP000194798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D3 {ECO:0000313|EMBL:OUD16186.1};
RA Fomenkov A., Vincze T., Grabovich M., Anton B.P., Dubinina G., Orlova M.,
RA Belousova E., Roberts R.J.;
RT "Thioflexothrix psekupsii D3 genome sequencing and assembly.";
RL Submitted (DEC-2016) 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:OUD16186.1}.
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DR EMBL; MSLT01000001; OUD16186.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A251XBT0; -.
DR OrthoDB; 9810730at2; -.
DR Proteomes; UP000194798; 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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00156; REC; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 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; PF00512; HisKA; 1.
DR Pfam; PF12974; Phosphonate-bd; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000194798};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..42
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 43..896
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012626025"
FT TRANSMEM 330..351
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 399..621
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 643..756
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 762..878
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 692
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 811
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 896 AA; 100918 MW; BD98DA18A749892D CRC64;
MSCYPCAFYW LCFFQGRQRG VLCRFLALML LCSFGGLNSA NANEVQEIRL VIQQHRTFIP
ELSATLAYLQ THFPDYRFTV QFMTTTALLQ AAAAGQLELA LTDAAVYLRL QHSYYAQHLL
TYQSAHPKTP YSQQASVIFT RADQHKLNNL SDLSNRRVMA TTNDGFSSWL PAWGLLLEAH
VSTRRDLRAL YFVKDDDEVI PAVFNQEVDA GVISAGSLER WLEQGKIQAD SFKILAAKPM
VEHFPFAHST PLYPHWAISA MPHLPKTISD GLTQHLLALS PNHPVVQQDA YAGWTVTANY
RVVQRLLQTL RLPPYEEFGK VTPTALLSQY GIWIFLTGVG FLLTIIASIH FKHLYDKLRT
MQYELHGELS ERRRTELALQ EAMAQAEAAN VSKSQFLANM SHELRTPMNA IIGYSEMLQE
EMQELGHSEY LTDLNKIYTA GKHLLGLIND ILDLSKIEAG KMELFLETFH LEEMLHDVIT
LIEPLVQKKH NTLEVHCIYD LGTMHADLTK VRQSLFNLLS NASKFTENGV IALYATRETV
EGVDWVIFRV CDSGIGMTEE QMQRIFEPFT QADASTTRQY GGTGLGLSIT RKFCDMMGGS
ITVESRPGDG STFIIRLPTT VAARHEDDSE EWLKLTPLLA VNKILVIDSD TAIRDHLKRT
LTREGFNVYV ADNVEHGLLL ARDLHPTAIT LDIQMAEADG WAMLATLKTD TELQHIPVIV
LSNLQNPETA YAQGAAEVFT KPVDQGLLAN TLKRYQLNHQ PCALIVEDDK STRELMHSLL
LKSGWRVAQA ADGEVALQHM QHDVPDLILL DLSMPKMDGF TFLDQLHRHA LWQAIPVVVI
TAHDLSRSER LRLAGKIETI LCKGAYTREE LLQKINGLIY AAAKMEARNK PQPLET
//
