ID I0GQY8_SELRL Unreviewed; 846 AA.
AC I0GQY8;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=SELR_14670 {ECO:0000313|EMBL:BAL83175.1};
OS Selenomonas ruminantium subsp. lactilytica (strain NBRC 103574 / TAM6421).
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Selenomonas.
OX NCBI_TaxID=927704 {ECO:0000313|EMBL:BAL83175.1, ECO:0000313|Proteomes:UP000007887};
RN [1] {ECO:0000313|EMBL:BAL83175.1, ECO:0000313|Proteomes:UP000007887}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 103574 / TAM6421 {ECO:0000313|Proteomes:UP000007887};
RA Oguchi A., Ankai A., Kaneko J., Yamada-Narita S., Fukui S., Takahashi M.,
RA Onodera T., Kojima S., Fushimi T., Abe N., Kamio Y., Yamazaki S.,
RA Fujita N.;
RT "Whole genome sequence of Selenomonas ruminantium subsp. lactilytica
RT TAM6421.";
RL Submitted (OCT-2011) 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; AP012292; BAL83175.1; -; Genomic_DNA.
DR RefSeq; WP_014424610.1; NC_017068.1.
DR AlphaFoldDB; I0GQY8; -.
DR KEGG; sri:SELR_14670; -.
DR PATRIC; fig|927704.6.peg.1517; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_336765_0_0_9; -.
DR OrthoDB; 9805486at2; -.
DR Proteomes; UP000007887; Chromosome.
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; cd17546; REC_hyHK_CKI1_RcsC-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 Gene3D; 1.20.120.160; HPT 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; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF79; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 315..535
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 568..684
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 737..835
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 617
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 776
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 846 AA; 94515 MW; 7A21754194DFCA10 CRC64;
MNNRKKMLLT ILMMLFLIFL SGIFIQQRIV NMLNKAAEHS VARQTEDLSM LAGERFRRFL
TPLQTAATHL SEHEEDKDDM LKMLVQQNPQ GQAGLIDFQH HTRGRSVSSK SFPRLQLAFH
GNTVIDYNPD IGILLATPVS YGDNVRYVLY QIYPISMLPQ LFALSDYDAF THVIIQYHDG
TLAVPYENYT TEDTRFWADE TIQSGMREVH SRLERNKAAA VYTEGAEGKY FVFGADLPQT
DFSLIGYMPW SAVAGQIMSI YQRVFFLFAL MLILFACLSI YLLMAQTSVA ETEELRQARL
AADAANLAKS QFLANMSHEI RTPLNAISGM NEMILRQQVP GEVRQYANNI KSATTALLTI
INEILDFSKI ESGHMEIVDT DYQLTNVLRE VCTLVGVRAQ AKSLLFKIHV DPYLPNGLYG
DAGRLRQILI NLLNNAIKYT PSGSITLDIS GQRKENTLYL QAAVTDTGIG IREEDKDRLF
HVFERLDIKR NCQIEGTGLG LAITYRLLNM MHGSIKVDST YGEGSVFTIE LPQEVHSFDP
VGVFSLSAQP DLDKVLEHQA SFIAPDAQVL IVDDNEMNCF VASSLLKETQ VQTVIAHSGA
ETMEALQKQR FHVVLLDYMM PGMDGVETLH KAKELPNIGS TRFIALTATA ISGSREKFLM
EGFDNYLSKP MTGDDLTNML LRYLPQELIQ HPLPAPAAAP IAAPSPAKTA EQASTTVAPP
APPLIDYKLG LTYCNNMQAV YDKILAMFNK QSSDKIAQLD NDLAAANWKD YRINIHALKS
TALTIGCRSL NQKAKDQEQA VKDYLAETAP PDQQQQAMDY IQQHHANVMD LYRQVAELAG
SPAQTG
//
