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Database: UniProt
Entry: A0A2N5N9K2_9BACL
LinkDB: A0A2N5N9K2_9BACL
Original site: A0A2N5N9K2_9BACL 
ID   A0A2N5N9K2_9BACL        Unreviewed;      1013 AA.
AC   A0A2N5N9K2;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=B8V81_1260 {ECO:0000313|EMBL:PLT47036.1};
OS   Paenibacillus pasadenensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=217090 {ECO:0000313|EMBL:PLT47036.1, ECO:0000313|Proteomes:UP000234789};
RN   [1] {ECO:0000313|EMBL:PLT47036.1, ECO:0000313|Proteomes:UP000234789}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R16 {ECO:0000313|EMBL:PLT47036.1,
RC   ECO:0000313|Proteomes:UP000234789};
RA   Passera A., Marcolungo L., Casati P., Brasca M., Quaglino F.,
RA   Delledonne M.;
RT   "Functional genome analysis of Paenibacillus pasadenensis strain R16:
RT   insights on endophytic life style and antifungal activity.";
RL   Submitted (MAY-2017) 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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00169}.
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:PLT47036.1}.
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DR   EMBL; NFEZ01000003; PLT47036.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N5N9K2; -.
DR   Proteomes; UP000234789; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 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; 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; IPR010559; Sig_transdc_His_kin_internal.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR34220; SENSOR HISTIDINE KINASE YPDA; 1.
DR   PANTHER; PTHR34220:SF7; SENSOR HISTIDINE KINASE YPDA; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF06580; His_kinase; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   SMART; SM00387; HATPase_c; 2.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 2.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Lyase {ECO:0000313|EMBL:PLT47036.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        203..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        232..249
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        269..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        300..317
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        355..378
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        390..408
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          434..645
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          678..795
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
SQ   SEQUENCE   1013 AA;  111516 MW;  5AB64168CB418A39 CRC64;
     MGVVGIVVLF GIWLPLGIFS ERWGGQQPFR AEQGVIDLAG WDGSGRIALD GEWEFYWNEL
     LQPGETPRGE RSWMEVPGVW SGSRAAGAER PVYGAATYRL RLTHLSEPGV YRIKKMNIRF
     ASAIYVDGRL VLEDGKPALS AEAYVPGNSP GLAVVEIKGS EAEIIVHAAN YDYIDAGVPM
     SLYFGKEEAI NAAHERSLIR ESAMAVVLAV IGLIHLVLFA AVWLYGQRDE PLLLFGLTCV
     TMAVFNGLLG ERPLALLLDG LSFQTLYTIK DMSALAGFLV SLYLMMLLQG KGADRRLTKL
     FALLLLGSLV LFPFLSIREY LPLYRVTILL EHVLMARVLW SAAARHLAAP RGQRYESLLL
     LLAVLLLNLY SYGCLLFGMS MLGSLLISQI YLILFSLVVF LVIVYRFYEA FRDMERMHRK
     LLRLDRQKDE FLSSTTYQLK APLQDIVHLA DSLAHADGPA PGSARSLALI AGTGRRLGYL
     VQDLHDFSRL KHEDIVPEPR NLDLRSAVGS VLELHRFLLS GRPIELANGV PETLAAVYAD
     EDRLEQILHR LVERAALRAE EGRIEVTAEE ELGFAVVTVD FDGRPRPAPD PDVAPCLAAA
     DGEAADLALS ITRRLIELQG GLALQPLPGK EGRSFRFSLL LEKNPAASRK AAWPAAGEAA
     AASETLVALA GGSRGQTVVL VAEPDAASRH AVCQLLAQEG LRAVSVRSAE QARAALALEG
     ELSLVLLGVS LADGSGFDAL EQLRNRFSPS ELPVLMLTGR RREEERRLAL DLGANDYISK
     PFEAEELLAR VRSLVKLRQS VREAREREIA FLRSQINPHF LYNALGAIAE LCVEEPEKAE
     RLTLHLSGYL RGSFDFGQRD GMSTLGAELR LIEAYTEIEK ARFGSRLQVT LRCEADPALR
     FPPLLLQPLV ENAIRHGLLS RPQGGEVKVT VVEREGYVHA AVEDDGAGFD AQAMLFRLEQ
     PERIGGVGLW NVSERLRLLY GERLGMDSRT GFGSRLTFRI PASSRTSEPK EGG
//
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