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Database: UniProt
Entry: A0A3N2MAA3_9BACT
LinkDB: A0A3N2MAA3_9BACT
Original site: A0A3N2MAA3_9BACT 
ID   A0A3N2MAA3_9BACT        Unreviewed;      1362 AA.
AC   A0A3N2MAA3;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=EEL33_07790 {ECO:0000313|EMBL:ROT07063.1};
OS   Muribaculaceae bacterium Isolate-037 (Harlan).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae.
OX   NCBI_TaxID=2486461 {ECO:0000313|EMBL:ROT07063.1, ECO:0000313|Proteomes:UP000275399};
RN   [1] {ECO:0000313|EMBL:ROT07063.1, ECO:0000313|Proteomes:UP000275399}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate-037 (Harlan) {ECO:0000313|Proteomes:UP000275399};
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:ROT07063.1}.
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DR   EMBL; RIAZ01000008; ROT07063.1; -; Genomic_DNA.
DR   Proteomes; UP000275399; 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; cd00075; HATPase; 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; 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; 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; 2.
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; 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:ROT07063.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000275399};
KW   Transferase {ECO:0000313|EMBL:ROT07063.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        779..801
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          837..1057
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1109..1224
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   REGION          1064..1106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1157
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1362 AA;  153670 MW;  845FD0C04C12B661 CRC64;
     MPRKTIILSL LVILFARISC YSSDSHLELR HLDAMPGSYN NLITALHKHS GGMLWFGTSS
     GLCRYDGYNV KQVNGGITDS TTILNDHILN IHEDCRGKLW LHSSDRYGVY DPVMDRLDIP
     DSESIVQKFG LEGFISNLTT DANGDIWLAL SGKGLYRIRC VDDKVEKVKG IPSTFAEITD
     MVIKDGELTA VDKRGALLFM DIEGMKVVST VAPDPIMNGN HLYEMYVDGD DRVWIYQMEL
     LYVYDRRNGK WLNDRIPNHG KIGIMKKIFQ DSSGRLWIAR DHHGLERILT TDEGLHFVPA
     DPPGMATRNN TITCFMEDSA GTIWMGTYKR GLLSHNESVR KFTLEEFPDV NCVTPASGND
     MWVGTDSSGL WIWDTKTGAR RRLSDPSFGE SEPAITSLTP DGNSNLYIGS FSKGLRLYDG
     KNFRKITTSS ALDDSYVWAS EFDSDGRLWC GTLGGGLFMY DPSTGEVVSY KNGTTELLSN
     YVMSVVLSRD KRVYIGTSYG ISVYDPKSGK LKRFRDLFPG IDTYRWKVSQ IYEDSRGLLW
     VGTSNGLKVI DRVHGKVQEI KLNDDGKQRY VLGITQDNGG SMWVSEGAML INIKVGYDEK
     TGNLNVVTHA YDNRDGLMEC DFNQRSFGKL PDGEIVVGGL YGLNRFSPSE MKFNMIHPRV
     VFTDLYMGSR LVRPGEEVDG RVVMKNGLAD GAEIEFSHNP KEFSIYFSTD DYALPEKTMY
     EYRLEGYNDE WTFCAPGVNH VTYTNLSPGK YRLLVRAVNG DGYESEEPGE LFIRVYPPFW
     TTTCAIVIYI LLGMVAIWGI VKIVSEMERR KFERDMHEEA MRKQEEINQL KFKFFTNVSH
     DLRTPLSLIV SPLEEMIKES TDERQTRRLT LMRSNAMRLL TLVNQLLDFR KNEVAGLQLN
     PTEGDVVAFS QNVCNSFVNL SERKNINLTF YSDRESISLM FDEDKLEKIF MNLLGNAFKF
     TPAGGRVDVS LEQVGEENPV LRIKIADTGV GIKDKDKEHI FERFYQVDDD GESHPHMGSG
     IGLSMVYEYV KLHDGTVRVT DNVDHGSVFI IDIPIRHIDR KSKGDVCREP KPVRQENVSV
     RPENVAEAAD ANSVEGSSGE GNAVDSRPLA LVVDDNPDMT EMLKFELEDD FEVITASDGN
     EALKVIENVT PAIILTDLMM PGMDGIELCR RLKGNKATVA IPIIILTAKH DLGVKLEGLT
     LGADDYITKP FNFNVLKLRM KRLVELTAKG ARRSLVDPEP EAIKITPLDE QFIEKAVKYV
     SDNIDSSELS VEELSEVLGM SRVRLYKKIK QITGKTPIEF IRVIRLKRAA QLLRESQLNV
     SEIAYRTGFN SPKMFSKYFK EEFGILPSVY QDKEGSETNY TV
//
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