ID S0GR53_9BACT Unreviewed; 1380 AA.
AC S0GR53;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=C803_03409 {ECO:0000313|EMBL:EOS16193.1};
OS Parabacteroides goldsteinii dnLKV18.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC Parabacteroides.
OX NCBI_TaxID=1235789 {ECO:0000313|EMBL:EOS16193.1, ECO:0000313|Proteomes:UP000014140};
RN [1] {ECO:0000313|EMBL:EOS16193.1, ECO:0000313|Proteomes:UP000014140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=dnLKV18 {ECO:0000313|Proteomes:UP000014140};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Xavier R., Kuhn K., Stappenbeck T., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Parabacteroides goldsteinii dnLKV18.";
RL Submitted (APR-2013) 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:EOS16193.1}.
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DR EMBL; ASSQ01000019; EOS16193.1; -; Genomic_DNA.
DR PATRIC; fig|1235789.3.peg.3413; -.
DR HOGENOM; CLU_000445_28_1_10; -.
DR Proteomes; UP000014140; 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; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17574; REC_OmpR; 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; IPR011047; Quinoprotein_ADH-like_supfam.
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; 5.
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; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 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}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 50..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 827..849
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 885..1098
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1130..1245
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1277..1376
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT MOD_RES 1178
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1380 AA; 158333 MW; F3D1646A293247F8 CRC64;
MCEYTIIYIN SESYSKNRGI AEMISYDIWF YVFFHHLCMK KTYNILQAVF MRKSILYLLL
MIICLSELYA ANRKSFNYYF SHISSADGLS ESQVKVILQD SYGFMWFGTK NGLNRYDGTS
IQTINCDDYI AGKGDHNISA LFEDENRKLW VGTDRGVYIY DPVYDLFTFI DQKTENGEQM
GNWVAKITSD HSGNIWILIP DQGVFRYKDE KLYYYAITNK DNIKRESPGA ICVRENGEVW
IGTAGVGLFL YNPQTDSFIQ HHTDKDGNTL MGAHIFSMCD YGDWIALAIH DGELKKYNPK
TNTLQTVNAP GVHHTILRDV VCYDQNNLWV CTHAGLFIVD EQSQKVTHLQ EDLMHSYSLS
DNIIFCIYKD REGGIWLGTK FGGVNHLPNY KLLFERFVPS SSENSLNTRR IRELAEDPEG
NIWVGTEDNG INILNPATGE VTQINYPESD RKSHLMTQSM SMYDGKIYCG LFKYGLDIID
ISNHSIKHLN HQQLNLDEES VYSQLIDSRG RLWVGNAWGL SRAEAGSFDF TRIPEIGLDW
IVCMLEDKKG QIWLASMGSG VWKYNPKDDS YKKYVNDTQD PASLSSNSVS SIMEDSRGQI
WFSTDRGGIC RYNEADDNFT TFSKEQGLPD DVAYKILEDK NHYFWFGTNQ GLVKFKPETG
DIRVFTTRDG LVGNQFNYNS GLKASNGKFY FGTIDGLIAF NPDDDQRTDS IPPVYITKFS
IYNKEVTVHT PNSPLNKSIL HTDRITLPYD QSNISFDIAL PSYSSARSKE CYYKMDPLDK
DWVKTSNNQN ISYAKLPPGN YTLLVKAEIE DDNQPVTSLR IVILPPWWLS SWAYAVYAIL
VLCLIYAWFR WYKRRKERQM EEKQKLFEIE KEKELYEAKV EFFTEIAHEV RTPLTLINGP
LETILDMNIQ DSKITRNLTV IAQNTKRLLE LTGQLLDFRK IGANKFKMDF AWTNVTTLLK
DTILRFEPTI VQQDKKLSVD IPEEEITAAI DREAVTKILS NLLNNALKYS AYTIHIELRR
EETTFSIRVT SDGNRIPAEL TQQIFEPFYQ INKKEGATTG AGIGLPLARS LAMLHSGKLW
LDTENSDNSF VLTLPLAQEK VRQQENSVIQ EEFIFPEEGT TVNVESRNYT LLLVEDNDTM
RSFLAEKLQE MFVMETAPDG KAALEILRNQ HIDIVVSDIM MPVMNGLELC KEMKADIELS
HIPVIFLTAK NDLDSKINGL RLGAEAYVEK PFSFNYLTTQ IFSLLNNRQK EREAFSKRPF
FPVNNMQMNK ADKEFMDKII AIIHENITDE NFGVEKLAEI LCLSRSSLLR KIKVLSGLSP
NDFIRLIRLK KAAELILDGK HRIGEICYLV GINSPSYFSK IFLKQFGVTP KDFEKQNQAS
//
