ID E7RM30_9BACT Unreviewed; 1348 AA.
AC E7RM30;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 72.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=HMPREF0663_10180 {ECO:0000313|EMBL:EFZ37811.1};
OS Hoylesella oralis ATCC 33269.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Hoylesella.
OX NCBI_TaxID=873533 {ECO:0000313|EMBL:EFZ37811.1, ECO:0000313|Proteomes:UP000005580};
RN [1] {ECO:0000313|EMBL:EFZ37811.1, ECO:0000313|Proteomes:UP000005580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33269 {ECO:0000313|EMBL:EFZ37811.1,
RC ECO:0000313|Proteomes:UP000005580};
RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., Hawes A.,
RA Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., Liu X.,
RA Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., Deng J.,
RA Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., Johnson A.,
RA Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., Song B.-B.,
RA Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N.,
RA Okwuonu G., Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W.,
RA Jakkamsetti A., Pham P., Ruth R., San Lucas F., Warren J., Zhang J.,
RA Zhao Z., Zhou C., Zhu D., Lee S., Bess C., Blankenburg K., Forbes L.,
RA Fu Q., Gubbala S., Hirani K., Jayaseelan J.C., Lara F., Munidasa M.,
RA Palculict T., Patil S., Pu L.-L., Saada N., Tang L., Weissenberger G.,
RA Zhu Y., Hemphill L., Shang Y., Youmans B., Ayvaz T., Ross M.,
RA Santibanez J., Aqrawi P., Gross S., Joshi V., Fowler G., Nazareth L.,
RA Reid J., Worley K., Petrosino J., Highlander S., Gibbs R.;
RL Submitted (JAN-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 -!- 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:EFZ37811.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AEPE02000002; EFZ37811.1; -; Genomic_DNA.
DR RefSeq; WP_004368851.1; NZ_GL833119.1.
DR STRING; 28134.SAMN05444288_0667; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG3292; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_28_1_10; -.
DR Proteomes; UP000005580; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; 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; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
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; IPR009057; Homeobox-like_sf.
DR InterPro; IPR018060; HTH_AraC.
DR InterPro; IPR018062; HTH_AraC-typ_CS.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR011110; Reg_prop.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR011123; Y_Y_Y.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF12833; HTH_18; 1.
DR Pfam; PF07494; Reg_prop; 2.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF07495; Y_Y_Y; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00342; HTH_ARAC; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 2.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS00041; HTH_ARAC_FAMILY_1; 1.
DR PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000005580};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 758..779
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 811..1042
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1091..1206
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1247..1346
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT MOD_RES 1139
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1348 AA; 153204 MW; B3698FE6DCACCCFD CRC64;
MQKYLVILYL VLFPLSAASQ FLLSRMVSSI SNLHVNDLVQ DDQGFMWIAT AKGLCRYDGV
GYNVFYHLQR QPRSIGSDNV NALYFDGRDL WCATGDGVSM FDMNTWQFTN YRMKHHMGSY
CLGFFFSGRH LYTYGYGGIY EVRKGSGRLV PVINFEGQVV QRAIVDSHGQ IWVVCDGNEV
MCFDASMNLC RKIDFGATKE VYSIYQAPGC NILLGTKNGL VALDKDTYTF LPSAVPPALM
HMSVKYIKGY APGKVVIGTK DNELKFFDFY KSNFIHFPNT DASLYTGIMD LTCSYADRSG
NLWLGTFNNG VKYLFQKKIF DTDEALIAGL KDKFVTRIRD DHHGNLWIGT RYSGLVRYNK
RGHAITEYNS RTSAIFRQLG NFIQSLFIDS SNRLWVCNEN SLLVFDITGG TLSLKKSFAD
VGNIVTIAED SRGRIWTGSS FKGITIYSSD LQMEKSFLPA TGKSNNITCL VPLSASTMLF
SVYGDNIYYI DVNSLRTRAL DPKYLTMFKN VVNMKRISGN RIVIGTYGNG LMVYHPQRRR
LAVFSYSDGL RSNDILGIEE DKLANLWVSS SFGLYRINLI TDKVRPYFMT DGTAGDQYHE
KSECMTDEGE ILFGGNHGVT QVLCRNINNT ARNVPVLLAD LKVFNKSVPI STEGEKGILT
RHISRTRKIE LKHDENVFSI DFIGLTYETP KNIEYAYKLE GFDKDWNYTG EYNRASYSNL
PAATYVFKVK IKNGADEWER EHTLLTIKVL PSPWMTPWVI MVYITLFFLV LFLINRVYIR
LKLKKERAIM ESNEIRREKR LAQMKVSFFT NISHELRTPL TMIYDPIKIL LKDKTINNPE
SQSLLTLIDK NSERLLKLVN QLLDYGRLKN DTLKLSVSDN DCVIQIVDIV NVYKLYAAEK
NITISLTCPY EQMVVFYDPD KMDKILNNLL LNAVKYTPMG GHVNVSVELE RRLIGSGDAS
TTRHFLVLEV EDDGNGVEES LLPGIFDRFK RLVKGDETSK IMGNGVGLNY VKHLVDNHKG
TITARNRAEK GMVFTVTIPV DETAYTADEI TFKDADSILA QRDGIFTGDD PFVNDTDTDA
ANELIVGERK RILVVEDNNE MVVLLRNILQ DHYTIDAAAN GIEALEWIRE SGPDLVISDV
MMPRMDGFAL CGAIKKDVML CHIPVILLTA KTLDKDKIKG YKEGADMYLN KPFNPELLLS
MIGNVFHRST YNQKLIARTS GGYTAEEREE LDKINSEMSP LDKRFLDRLN SYIDKHIADS
DLNVNTLGRD LGFSRTNFYR KVKSLTGMMP NDFLRVFRLN RSVELIKLRE YPLNEIGFMV
GFGTQSHFSS CFKKHFGISP KDYLTGYK
//