ID A0A1M4WBB8_9BACE Unreviewed; 1354 AA.
AC A0A1M4WBB8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05444405_10341 {ECO:0000313|EMBL:SHE78551.1};
OS Bacteroides luti.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1297750 {ECO:0000313|EMBL:SHE78551.1, ECO:0000313|Proteomes:UP000184509};
RN [1] {ECO:0000313|EMBL:SHE78551.1, ECO:0000313|Proteomes:UP000184509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26991 {ECO:0000313|EMBL:SHE78551.1,
RC ECO:0000313|Proteomes:UP000184509};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FQTV01000003; SHE78551.1; -; Genomic_DNA.
DR RefSeq; WP_073399280.1; NZ_FQTV01000003.1.
DR STRING; 1297750.SAMN05444405_10341; -.
DR OrthoDB; 717811at2; -.
DR Proteomes; UP000184509; 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; 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; IPR013783; Ig-like_fold.
DR InterPro; IPR011044; Quino_amine_DH_bsu.
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; 2.
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; SSF50969; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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:SHE78551.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000184509};
KW Transferase {ECO:0000313|EMBL:SHE78551.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 775..793
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 829..1065
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1106..1221
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1254..1353
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT MOD_RES 1154
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1354 AA; 155630 MW; 7FA6725B51FC4D67 CRC64;
MQKLLSFFML LLFLIYVTSC RPKENANENK TAIASPVIAN DISNQKISSF AEDAQGHIWI
GTFRGLNKYN VHEFHQYFCT DDSLDLPDNQ IQDIFRDSQN RLWISTVNGA CLYTDKDNFQ
RIPITIPNQN GTQFLEDKNG KIFLNMVFQL CVYNSEKKQF DCAIKAFDPQ GTFSGRCYID
NNNRLWAVNP LALRCYNSST IKLEDSIPTK HSVYYSYMRD NGELWLVGEN SLSVFDTRTR
KYIDVPKVIR NHPVLSKSTI NYIYPYENNS LLINTTENGM FLYNYIEGFV IHQDENGFPF
EVPHFKISKM FTDSQKNLWI GSVDQGYVVR YNYKKRFNNN NYLCSCVKQK SVVAVAIDKE
KHLWISTLMD GLYMYDLDSR KVEKINMQKI LPQDNQENHD VSYLFVDESN AIWMVVSSNK
VMRCRYKNGM LQVEATYPIL FPMCITQDRN NTIWVSTASQ FVYALRQRET KFKPIQLYNK
GFIFIPGMLP LSTGEILFAA FNNSMQLVDP NTWKPKELKI SKEDIKSCIP RSVFIPTKLY
EDTNGDIWIG TVSNGLMRYS PSTKRMYPIS GISCTDISSI EEDRQGNIWV STQYGLYKYD
RTVGKFTSYY AADGIGGNQF YERTSCRLPN GALVFGGTHG LTVFDPIDVT FKRNIPLLFE
DLKIHNKLIR PQNESCIDKH LSYKPDIHLD HDQNSFSISF AALDYCEYER VHYCYKLEGF
DKYWIDAGNN REAYYANLPV GTFTFKVKIT NNDKTIVEAE NSLQIIVSPA PWATWWAYCI
YFIVIAGVIY LLFSAYLRIK TEKEAALRAE QEKAQEQRVN KMNMSFFSNI SHEFRTPLTM
ISGPVAQMCD SPEIKGENKK LLYIVQRSVD RMLKLVNQLM DFNKLENDTL RLKVKRMDVI
SILQQLTDVF KVNAQNKNIT LSTFGLEDSF ILWLDEDKVD KIMGNLLSNA LKFTPIGGKI
DIDFDVITRD DALKQFSLTD KDVDIQYIKV TVTDTGKGIP ENQMEKIFIK YYQVEDQSEG
TYNWGTGIGL YYARSLAELH HGYLKASNRK VGNGAIFTLI LPINEISYTE EERSVEQGTQ
EDVFPLSDKK PYKQVENLNS TGKQQTLLVV DDDTEVAYYL KAMLSSYYNV ICRFDANSAL
EAINEEVPDL ILSDVVMPGV DGYQLCRQIK EDLLLCHIPV ILVTAKTTVE NQVEGLDIGA
DAYVTKPFDP NYLLALIKSQ LKNREKIRNI LGSTTQTNNI SKNVLSPQDN AFMTDLYHLM
ESELSNTELD IVHMTARLKI SRTKLYYKIK GLTGENPGVF FKKYKLNRAA ELISEGKYTI
SEIADMTGFT TLSHFSVTFK KHFGIVPSEY KGIN
//
