ID A0A133Y220_9BACT Unreviewed; 1334 AA.
AC A0A133Y220;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=HMPREF1870_02372 {ECO:0000313|EMBL:KXB37228.1};
OS Bacteroidales bacterium KA00344.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales.
OX NCBI_TaxID=1497954 {ECO:0000313|EMBL:KXB37228.1, ECO:0000313|Proteomes:UP000070254};
RN [1] {ECO:0000313|Proteomes:UP000070254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KA00344 {ECO:0000313|Proteomes:UP000070254};
RA Mitreva M., Pepin K.H., Mihindukulasuriya K.A., Fulton R., Fronick C.,
RA O'Laughlin M., Miner T., Herter B., Rosa B.A., Cordes M., Tomlinson C.,
RA Wollam A., Palsikar V.B., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-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};
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:KXB37228.1}.
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DR EMBL; LSCT01000212; KXB37228.1; -; Genomic_DNA.
DR STRING; 1497954.HMPREF1870_02372; -.
DR PATRIC; fig|1497954.3.peg.2427; -.
DR OrthoDB; 717811at2; -.
DR Proteomes; UP000070254; Unassembled WGS sequence.
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; 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; 4.
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; SSF101898; NHL repeat; 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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000070254};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1334
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007460196"
FT DOMAIN 832..1044
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1081..1196
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1228..1327
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT MOD_RES 1129
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1334 AA; 152505 MW; B348AD6AEBB7C3A9 CRC64;
MKKDTFIFLL LLIMGMSSST ATSIRPGRYL LNHIDGRSGL SENMVKSILQ DSWGFVWLGT
KNGLNRYDGF NIKHYDVDDV QKKVGNHNIS ALYEAPDHRI WVGTDKGVFV YNRYQETFDF
FDKKTDKGVD VSNWVNQIVG DKHGNIWIIV PNQGAFRYDT RKKKLHLYST SREKETYEHN
IQSMCLRNDG TVWFGTDGNG IFKYNYQNDK MEDVLPKSLK EALANKNIFT MTDYGEWIVL
GEHEARLEKY NPTTKELKDV DAPNVHYKVI RAVAYDGDKL YVGTQDGLFI IDETKQTEEQ
LKENIAEPFG LSDNMIYSIY CDRHNGIWIG TMHSGANYLS KGGMHFTTFF PSATPGSLSS
KLVHEMVGTD NGDVWINTED GFVNIYHPAI QTFENVEVPI YKGGTGRLAL MNNGTEIWSG
LFKNGLDVIT ISNHTVRHYS PQELQLDAEP SVYALYKAHN GKVWLGTARG IYIQDKDMRF
TKVKSIPDMY TQDIVQDQQE NIWICTIGTG VYRLNLRTGR VSHFTHHADD PKSLSSNDVS
SVTIDHLGNL WFATDRGGIC KYDAQLDHFV SYGKAEGLPD DVAYKIIEDV NHFLWFGTNQ
GLVRFNPTTL DVTVYRNTNG LFSNQYTYKS AYKHPDGTFL FGSYSGLVAF NPQPANKNLS
KHRIYITNIQ VDNIEVKPGV GDVLETNIVH ARKIKLPYDF SSLHLDISSM NFSGSEAANY
EYKIEGVDKK WNSTTASVGI NYTRLQPGRY KLKIREAGYT SNMVTLNIIV LYPWWSSVWA
RLIYLLVAVL LGWYLYKSIK QRQRRTLSIR ASRLREAQEK ELLQSKISFF TNITHEIRTP
LTLISGSLEN IHDEKIEDKG IEKSIRAVKL NCQRLLNLID QLLDFRKMDA KSLQMNFVNM
DVCELVRNII THFEPTIVNQ NKTISLDVEE DSITLPINPE ILTKIISNLL NNAMKYSETF
IQVNIRRTSD SLLLTVLNDG QKIPIDKVEE IFVPFTRLDH NDSKTGTGIG LPLARSLAEQ
HNGSLTLDTT SEYNSFVLNL PLYQDNVMKL DKESLNMNET SLDSIVVEDF HVDNTNKKEH
TLLIVEDNAE IIDLIRDNLG EYYNVLIAYN GEEALEMMND HRVNLIISDI MMPVMDGLEL
TRRIKSDFKL SHIPVILLTA RQTLGDNIEG LQAGADAYIK KPFNFVYLQT QIKTLLDNRK
REQESFLHMP HLLIENSGIN NVEEKFLNKI SNLIISNMHD PSFNVERLAS EMCMSRSSLH
RKIREVSNLT PIDFIRLIKL KKAAELIREH GYRTTEVCDK IGISSPSYFI KLFQKQFGMT
PKEFASKKTD AHTK
//
