ID R7AXF0_9BACE Unreviewed; 1341 AA.
AC R7AXF0;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BN800_02462 {ECO:0000313|EMBL:CDD51287.1};
OS Bacteroides sp. CAG:875.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1262752 {ECO:0000313|EMBL:CDD51287.1, ECO:0000313|Proteomes:UP000018287};
RN [1] {ECO:0000313|EMBL:CDD51287.1, ECO:0000313|Proteomes:UP000018287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:875 {ECO:0000313|Proteomes:UP000018287};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CDD51287.1}.
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DR EMBL; CBHD010000174; CDD51287.1; -; Genomic_DNA.
DR Proteomes; UP000018287; 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; cd00063; FN3; 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; IPR003961; FN3_dom.
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; 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; 3.
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 Coiled coil {ECO:0000256|SAM:Coils};
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 780..801
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 834..1052
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1085..1200
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1239..1338
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT REGION 1055..1077
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 887..921
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1055..1073
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1133
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1341 AA; 152862 MW; 2509ADD7E1EAC5E7 CRC64;
MRNNLILLCL LILGEFQSIF SQTQYTFKRL TMTDGMVSNY IVDVIQDKQG YIWMASESGL
CKFDGKDFTI YNTGNSAIKS NAHNVLYYNE ADNTVWVGTQ RDGACIFNCE TQTFTNLKGM
MTEDVTDLSP SSDGGIWITH YHLGIDYYSN QTKQITHYKA KDIKGLDFGH FWCAREDKNG
HLYAGLQKGG LAVIDIKKRT AKIYRHDPND PHSIPNNTVH CIFISKTNSV WVGTEDGLAL
FNPQKEQFIS FQNQPNNPTS ILSNQINDIG ESKDGKLWIC TQMGGVSILD LNDNVFTSPE
HMHFQNIKAT NDLHGISSPN AKSFMQDSFG NIWIGNYRGG VDFLSYDKPI FQTLEYNILK
DGALTDKQVW GLTIDDESQV WLGGEHEIAV FNEKMQLQKI IPLTGKANPH THASVIFKDK
HGMLWLGLYK DGILTCNPKT EAIVRIPIDD KDAEICCIYE DHNKIWIGTQ NGLYSWENGI
ISEEKTINEQ LSDLMIHGIQ KDHQGRLWLG TFGKGLAVFS PQKQLIMKFD TTNGLATNAV
NSLYLDKKGG LWAATRAGIA HIDNTSKPQI EILDHRQGLI NENVRAIIED KQGRIWLSTN
GGIAQWKEKE KKFLNYTWHQ GVPRGDFMDG AVCIGMDGTL FFGSQNGACY FNPEDIVENI
PIAPVQITCV RSYEYSNPNS KGSIIPIIDG KANLSYRNST FTVTFSVMDY TQSPQVEYSY
TMEGLGKTWF EVENENRITF RNLPPGEYTF KVKARMRNQE WGNDFSAIHI TIDPPIWLTW
YAKLGYFITI CLIMYAILYF YKRKLALESR LNLEHHQHEN DQKLNNERLR FYTNITHELR
TPLTLILGPL EDLQADKTLS SRQVNKISII RDSANRLLNL INQILEFRKT ETENRKLKVR
YDNLTRLIQE IGIKYKELNQ NPNVEIHIKT DSQDASLYYD QEIITIIVDN LMSNALKYTP
KGVITLSIDS CEKNDIKYTT ISVEDTGHGI SKESLNHIFE RYYQGQGKYQ ASGSGIGLAL
VKSLADLHQA TIEVESEVEK GSKFTLRLLT ENTYPNAEHP TIKTDTPLQE SISNEQKETE
DGKSIILLVE DNQDIREYIR SSFEDRYEVI TAADGKEGWE IAQNQIPNIV ISDIMMPIMD
GIELCRNMKK DVRTCHIPII LLTAKDTLQD KEEGYAAGAD SFITKPFSAK LLNSRINNIL
ENRRKIAGLI TAIPETENEQ KDIENERKNL NKLDQEFLDK VTGIIEENLS IEKMDVAFIA
DKMCMSHSTL YRKIKGLTEM SVNEFVRKIK MKKSIELINS ENYSLAEISD LTGFSSIAYF
RQCFKDEYGM APTEYLKKKR K
//
