ID A0A1R3T5A8_9BACT Unreviewed; 1356 AA.
AC A0A1R3T5A8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=PSM36_0941 {ECO:0000313|EMBL:SCD19767.1};
OS Proteiniphilum saccharofermentans.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Dysgonomonadaceae;
OC Proteiniphilum.
OX NCBI_TaxID=1642647 {ECO:0000313|EMBL:SCD19767.1, ECO:0000313|Proteomes:UP000187464};
RN [1] {ECO:0000313|EMBL:SCD19767.1, ECO:0000313|Proteomes:UP000187464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M3/6 {ECO:0000313|EMBL:SCD19767.1};
RA Seilhamer J.J.;
RL Submitted (AUG-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};
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DR EMBL; LT605205; SCD19767.1; -; Genomic_DNA.
DR RefSeq; WP_076929282.1; NZ_LT605205.1.
DR STRING; 1642647.PSM36_0941; -.
DR KEGG; psac:PSM36_0941; -.
DR Proteomes; UP000187464; Chromosome i.
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 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; 2.
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; 8.
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; 4.
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:UP000187464};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 795..816
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 849..1067
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1102..1217
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1253..1352
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT MOD_RES 1150
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1356 AA; 154980 MW; E82EE77851FB48FE CRC64;
MKGIKRETFL ILILVVTMAG LQAQPSVITS LGREQGLSNN YVVSITQDKD GFLWFATEEG
LNKFDGTRFT SYYKHTGNIS GNELNYIYAD PVEPVIWIAT QRAGLDAYNY EHNTLEVFTH
NDESPSSLIT NDITSITPAA DGNLWISTYY RGVEYFNKRT KEFTHYNTET LPDLVSDMVW
TILDDHNGNL YIGHVQHGMS VLSLNDGQVV NFRNNPSDKE SIPGNEVRCI YKDPNNNIWV
GTDKGLALFN SDAGKFISVD SSSQGILTSR IFDIRQMNDH KLWVATELNG IAVIDIKQHF
FMPSGQPSIQ HYMAGHNKYS LSVATVRSIF QDSFGNIWLA TYGGGINFIG HTQPLFESYG
YSPLPDDVNS LNNRIALSLC LDNDEKLWIG TDGSGVNVFE NGQRIRIYNK ERGTLTHNTI
QTMMKDSRGN IWLGSFLTGI DFYDHQSKRF QPIVVNGGRN WDVRCFFEDA DANIWVGTQE
GIWVLDGKTR RMIHHYDTKN NQLPEDQVRA INQDHLGRMW IGTFGLGLAV YTKDMQLLAD
FNEYNNFCSN TINQIFRDSY GEIWIATGEG LVRFAEHDSF HYEVFQRDNG LHNTNIRAIT
EDGAGNIWFS SNDGITCYVR EKKQFYNYNL LDKSPMGSFS SGAVTKDKKG SIYFGYNKGV
CYFNPAFVLE ERIVPQVVIT DMKIYESGVA PKNDQHINSF VEKNRHIVLN HKQNTFSISF
NIQDYSLTNH VDYAYMLEGL DEVWHTVNDN TVMFRNVPPG HYKFLVNTRI RNQEWSPESI
YPLSIHIQPP LWLTWWAKTL YVAAGLLIVF FFLLAYKKRL EMQSSYELEK NNREQEQELN
NERLRFYTNI AHELRTPLTL ILGPLEDLQK DGQLLSRQQQ KISIVRQSAL QLLNLINQIL
EFRKAETQNR RLCVSKSNLA VLVKESGLKY MELNVKQNIQ FGINIEDEEM FLYFDKEIVN
IILDNLISNA MKYTDKGSIK ISLYTTMRNN LSYTEIKVED TGYGISKEDQ TRIFDRYYQA
KGTRQVPGTG IGLALVKNLA DLHEGEIRVE SKINEGSSFY FSLLTHNIYP NALHNDREEE
IPESAESINE SAEETKSNGK PILLVVEDNP EIREYILDSL SDSFHVITAG EGEEGCNAAF
AHIPDIIVSD IMMPGMDGIT FCQKIKADVR TSHIPVILLT AKDSLQDKEE GYRSGADSYL
TKPFSASLLH SRINNLLETR KRLATQFVLD SGKDEKSALF KESLNKLDNE FLENLTRLIE
ENIQSEKVDI SYLSGKLFMS NSTLYRKVKA LTGISTNEFV RKVKMNNAER LLLTGKYNIS
EVSFRVGMNS PVYFRQCFKE EFGLSPSEYL KKIKME
//
