ID A0A3N2MTE2_9BACT Unreviewed; 1335 AA.
AC A0A3N2MTE2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=EEL48_07900 {ECO:0000313|EMBL:ROT13442.1};
OS Muribaculaceae bacterium Isolate-102 (HZI).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae.
OX NCBI_TaxID=2486470 {ECO:0000313|EMBL:ROT13442.1, ECO:0000313|Proteomes:UP000272558};
RN [1] {ECO:0000313|EMBL:ROT13442.1, ECO:0000313|Proteomes:UP000272558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate-102 (HZI) {ECO:0000313|Proteomes:UP000272558};
RA Clavel T., Strowig T.;
RT "Sequence and cultivation study of Muribaculaceae reveals novel species,
RT host preference, and functional potential of this yet undescribed family.";
RL Submitted (NOV-2018) 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:ROT13442.1}.
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DR EMBL; RIBI01000004; ROT13442.1; -; Genomic_DNA.
DR Proteomes; UP000272558; 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; IPR018062; HTH_AraC-typ_CS.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR011110; Reg_prop.
DR InterPro; IPR013658; SGL.
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; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF08450; SGL; 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 DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Kinase {ECO:0000313|EMBL:ROT13442.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000272558};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:ROT13442.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1335
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018087902"
FT TRANSMEM 784..802
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 1087..1202
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1234..1333
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT MOD_RES 1135
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1335 AA; 150011 MW; 90F1057743B53599 CRC64;
MKKLCLLFIA GLMSLAALAS GSNLAFRHYT TDNGLPSNCV RDIMQDSRGF IWFATDGGLV
RFDGQRFRVF SLSKVEGKHS QDDFVSSMHE LDGKIWIGVD TQLFYYDPET EKILAPELHY
APACTSRIDS YVRDMTSDKD GNLWLAVAGN GVFKVNSVTG DVVNYEFPQL SNMVGRIYVD
SRNDVWVMGN QGRGILFKLN KSDDTFKPLQ LKLDGRPLHV IAVAMVEDEA HNMWIGMWDS
GLYRFDPFTG EAYAALQPGA DRGLVHIHSI TAGSNDALFI GSDAGLTVFN PKSGEYTLYK
NDELDRRSLS DQFVYPILRD REDGMWIGTF YGGVNYLAPD LKQFNAHRHS RFVNSVSGDI
ISGFCEDGMG NVWIASDDGG LCYYTPSTGR YSHVALPSTG AVPFNNNVHA LCLDGDDLWI
GTYTTGVGVY NIKTHLMRHY YPREGDDSSL DGWSSYAIYR DRDRNIWVST MDMINLYDRE
ADNFKRVRSL GAMTIDIDQD VLGNLWFSTQ GKGLFRYDTR HRVWKNYRFS GDEGALPHNH
VNCTTIDSRG RMWVATANGL CRYVPERDSF EIINIGDVPS KIVFSVIEDQ NSLWLTTSNG
LVRYSLVDGS SELFTTFDGL SNNQFMLNAG LKTSSGCIYL GTIKGLNSFY PYQIRPNQAM
PPVAFTELDV VNSVVEVGDS RLPKSLNSVE RIELSHEDYL FSLSFSALSY VNPSKNHLRY
KLEGFDKTWI NAGSDNRATY TNLPPGNYRM MVQASNNDNL WNEDGITLHI KILPPWYASI
PMKILYVLLA LGLIFLLIRL LLRYYDKQHK VELSRVSANK EKEVYQAKMS FFTMIAHEIR
TPVSLIIGPL EKIMRSPGEL SPTVRDDLNI INRNSQRLLF LVNQLLDFKK VEQNGFTVQF
SRQNVTNLVT AVAERFAPSI EQMGGKLVVE QCERDIEADV DAEALTKLVS NLLNNARKYM
KDRIVIACHA DEGQGWFTIS VSDNGVGISR DNQEKIFKPF FQVMDDNRES KGGTGLGLSI
VQSVVEAHKG EIKVESSLGN GATFIVTLPL RQEGVTASAG NDIMSPAEDK GCSRAIDGGV
NDVSRPVMLI VDDNEEMLQF ITSNFNSDYE VVTAVNGKEA LDKLSRHEVA LIVSDWMMPV
MNGVELCRAV RSNCNYSHIP FILLTAKTDN YSKIEGLNCG ADAYVEKPFS VNYLEARIHN
LVEMRKLLRE KFSQTPLEPI NTIAPNPVDD QFLTQLTNII EENFSNPELS VDFLANRMGI
SRSGLYAKIK TLANVTPNEL IQLTRLKKAA KLLAENKYRI NEICYMVGFN SSSYFSKCFQ
RQFGIKPGEF TPHSL
//
