ID A0A0F5JFP9_9BACT Unreviewed; 1319 AA.
AC A0A0F5JFP9;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=HMPREF1536_02282 {ECO:0000313|EMBL:KKB56646.1};
OS Parabacteroides gordonii MS-1 = DSM 23371.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC Parabacteroides.
OX NCBI_TaxID=1203610 {ECO:0000313|EMBL:KKB56646.1, ECO:0000313|Proteomes:UP000033035};
RN [1] {ECO:0000313|EMBL:KKB56646.1, ECO:0000313|Proteomes:UP000033035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS-1 {ECO:0000313|EMBL:KKB56646.1,
RC ECO:0000313|Proteomes:UP000033035};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Martens E., Sakamoto M.,
RA Benno Y., Suzuki N., Matsunaga N., Koshihara K., Seki M., Komiya H.,
RA Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Parabacteroides gordonii DSM 23371.";
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:KKB56646.1}.
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; AQHW01000014; KKB56646.1; -; Genomic_DNA.
DR RefSeq; WP_028728047.1; NZ_KQ033919.1.
DR STRING; 1203610.HMPREF1536_02282; -.
DR PATRIC; fig|1203610.3.peg.2343; -.
DR HOGENOM; CLU_000445_28_1_10; -.
DR Proteomes; UP000033035; 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; 3.
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}; Reference proteome {ECO:0000313|Proteomes:UP000033035};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 768..791
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 826..1041
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1071..1186
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1218..1317
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT MOD_RES 1119
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1319 AA; 150793 MW; DD6623DE7475A6FB CRC64;
MSYLKLILSI LFLSCSLWIF ADESNYLFRH YQVENGLSDN MVTGCVQDKS GYIWIGTRDG
LNRFDGYTFK VFRNDPDDAE SLGNNWVTHL NCDNEGNLWV GTLSGLYQYN ETKESFLHVP
FTKNKGIDLF QFDENNLLWL LMDGALIQYN IADGQFHIFT GNNGQTYTSF CIMPDNSIWL
GDSEGFISLL NTEDGTLDSY DLFAHSPATT SRKLSMLYRS PSSANIYVAF EHDDVKIFNV
LTKTYQDLNI QEKNQLTILI NCFLEKDKEE LWIGTDSGLF IYDLQLGTCK RIRQDPLDPY
ALSSHFVSAL FEDREEGVWI CFHQNGLNYY SPFRPFNVYY PWNETHSLKG EVIRDICSDA
YGNRWIGTED AGVNCMEKKT ETFTNYQPVP GVKSLSHTNI RGLAASGDNL WIGHVIHGID
LMDIKTRKVI KHYDLLKDSH TVKNSTVRCI KVLREGEILV GTEDGIFRYD YLNDRFVYAS
QFPPFAVNSL YEDRAGKIWL GMFNRSYYFN TTSNTGMYLP YDKLNTQRHN TVNDACEDKD
GNMWFATVEG VIKYDFQTGE SLHYTVKNGM PSNVAFRILP DENNCLWIST ANGLVCLNTQ
TEKIMTYTEA HGLVTRQFNY NSAFKDDDGT LYFGTVKGFI HFKPGDVKPA AEKMDVHISS
LDIQNGTGGR QIINSSSSSE VKRITLNHGQ STFNINFSSL NFIAPKSIQY AYRMVSLDRD
WIPLGERNIV YFTELHPGDY TFEVRAANLS NNWEGKITRL HITVLPPWWV STSAYIIYSI
IILAVIIYLI FYWRRKNKRS MAYNMQIFES KKEKELYQAK IDFFINIAHE IRTPLTLIKN
PLERLLRSDK IGEKENNSLI LMDKNVSRLL SLVNQLLDFR KTEIEGYRLN FIRTEVVSLL
TETAKRFQEI ATENNLLLNL DLTVQELYVF VDREALTKIM SNLFSNAVKY AAGSIVVRLQ
PSADYETFTI DFINDGVPVP AEMRDKIFEP FYRIKGNEDK PGTGLGLPLA RSLAEMHHGT
LCLADTSGNQ TLFRITLPVK PVGAVKTTEE EVQSLPESRK ITYTREEGRP TILIVEDNKE
MSAFIADEVN ENYNVLIAGN GSEALEQLKK ESIQLIISDV MMPVMDGFSL LRSVKTDIEF
SHIPVILLTA KNTMQARLEG LELGADAYID KPFSTNLLMA QISNLLSNRD NIRKFYFNSP
IANMKSMAYT KADEGFLEKL NEIINENIGN PELDVNMIAD LMHLSRPTLY RKIRAISDLT
PNDLIKISRL KKAAELLLQG NMKIYEISEA VGFSSQSYFW SAFIKQFGMS PSKYAKENR
//
