ID R6MZC2_9BACE Unreviewed; 1328 AA.
AC R6MZC2;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BN659_00514 {ECO:0000313|EMBL:CDB99461.1};
OS Bacteroides sp. CAG:443.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1262739 {ECO:0000313|EMBL:CDB99461.1, ECO:0000313|Proteomes:UP000018098};
RN [1] {ECO:0000313|EMBL:CDB99461.1, ECO:0000313|Proteomes:UP000018098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:443 {ECO:0000313|Proteomes:UP000018098};
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:CDB99461.1}.
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DR EMBL; CBEN010000087; CDB99461.1; -; Genomic_DNA.
DR Proteomes; UP000018098; 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 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; 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; PS01124; HTH_ARAC_FAMILY_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:CDB99461.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:CDB99461.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 770..789
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 824..1038
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1074..1189
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1228..1326
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT REGION 1049..1068
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1122
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1328 AA; 152870 MW; 30975649CFDA99F0 CRC64;
MFLFFLCTRV APAELFPSFV INSYTVKNGL SHNTIWCALQ DSYGFIWFGT DNGLNCFDGQ
RNTIFRTSSQ NKKQSLGSNF IYSLFEDKQR RIWIGTDRGI YIYDRKNTFI PFTQMTKFGV
SISSEVRKII QLSDEEIAIA TLGQGIFIYN LQNDTLTQNN QYLSFVWDMY VDRNHKLYIA
SLQEGIICLD KGQKFIQSFP LQTKEQTKNY LKTNCILPIG KSLWIGTDSK FLFEINTLTG
KVDCRKLQSD QFQIVQCLIP FTKDTFLIGT DNGIYLYNYK DQTLSNLTEI HNNDGTNITD
QNINAFIKDK EGGIWALTNQ TGAIHIIPKN KTFNLHKIPG NPTVNAFYED HKRHIVWVGT
QKGLFTYNTT SNDIQEYPLV EKEKQLYDIR CLCLKEDELW IGTFSNGLKV LNLTNGKIRT
YQHSYNIPNT ICSNNIQKIY KCHDGTIYIG TNWGLCYYNP EEDNFRTETS VGAMISITDI
YEDSHNNLWI TTANNGIFFN NKNANYWKHY EHKQGVESSL INNSIITLFE DSNKKIWLGT
NGNGLCLFNA EEETFTTFTN KQLSTLVVYS IEEDFYGYLW LTSNIGLIRV NPKNFDDYQY
FTNSDGLQEN LFCERASHKI SDGTLLFGGT NGFNSFQPSF VQKNTFIPPV YITDFILTHS
DSSQDTQELL NLEEPIFLTK QIKLPFNNNS FSIYFASLSY QNPQKNHFSY KLEGVDTEWN
SNIRENFATY HNLPPGKYCF SVKGSNNDQK WNEQIAKLWI IITPPWYRSV WAYLAYIACA
ICLIIYVLYK RDFYLKAKYQ KRIEEYQIKK DKELYKNKVN FFINLIHEIR TPLTLIKLPL
ESIMHAAIDK QTEEHYLQVI NKNVDYLLGV TNELLDFQKM ESGEIKLHLK LCDISQQINS
IYQQFAGSAD LRNISLSIHQ PEDFHLEALV DGDKLNRILV NLLSNAMKYA NNVISITVKN
DAKEFSIIVE DDGPGIADAE KEKIFQNFYQ VADGQSIQGT GIGLAYSRAL AESHHGTLHV
ENSSLGGSAF ILTLPIYNED LQKEENKGII LPDSRSHTDL EGSNDKPASS SKAKILLVED
NRDLLELECN GLKEYYHILK AQNGIEALQI MKDEDVDIVV TDVMMPLMNG FELCHKIKSN
IEYSHIPVIL LTAKTLPESK EEGFSYGADS YIEKPFTIQQ LHMQIRNLLN LRTAFQKRMA
SFFPQATPEE KDKEDYIPFT AQDQEFIKKI QEIIELQLND ENFSIDVLAT EMHMSRSNFY
RKLKALSGMS PNDYLKNCRL NKAAQLLKEG YRVTEVFERT GFGSSSYFAK CFKAKFGVLP
KDYTESLN
//
