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Database: UniProt
Entry: A0A0M9DKJ5_9BACI
LinkDB: A0A0M9DKJ5_9BACI
Original site: A0A0M9DKJ5_9BACI 
ID   A0A0M9DKJ5_9BACI        Unreviewed;      1022 AA.
AC   A0A0M9DKJ5;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=ADM90_10390 {ECO:0000313|EMBL:KOY82052.1};
OS   Lysinibacillus macroides.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX   NCBI_TaxID=33935 {ECO:0000313|EMBL:KOY82052.1, ECO:0000313|Proteomes:UP000037977};
RN   [1] {ECO:0000313|EMBL:KOY82052.1, ECO:0000313|Proteomes:UP000037977}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 54 {ECO:0000313|EMBL:KOY82052.1,
RC   ECO:0000313|Proteomes:UP000037977};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Che J., Ge C., Shi H.,
RA   Pan Z., Liu X.;
RT   "Genome sequencing project for genomic taxonomy and phylogenomics of
RT   Bacillus-like bacteria.";
RL   Submitted (JUL-2015) 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:KOY82052.1}.
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DR   EMBL; LGCI01000006; KOY82052.1; -; Genomic_DNA.
DR   RefSeq; WP_053994956.1; NZ_LGCI01000006.1.
DR   AlphaFoldDB; A0A0M9DKJ5; -.
DR   STRING; 33935.ADM90_10390; -.
DR   PATRIC; fig|33935.3.peg.3980; -.
DR   OrthoDB; 9809348at2; -.
DR   Proteomes; UP000037977; 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:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 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; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR010559; Sig_transdc_His_kin_internal.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR43047:SF83; HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 2.
DR   Pfam; PF06580; His_kinase; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 2.
DR   SMART; SM00388; HisKA; 1.
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; 2.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KOY82052.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; 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        5..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        207..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        238..254
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        274..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        303..320
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        340..358
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        370..391
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        397..416
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          445..661
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          697..813
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          924..1020
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   MOD_RES         746
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1022 AA;  116117 MW;  0381429DE0BAAD00 CRC64;
     MKKNILIIAC IIMLFSIVFF LGNWHYFSDK NPRIVEDGAV TIEAEQLQKN KIVKLDGEWS
     FYPNVLIPPQ ASLDSYEDER IAIPVPTKWH KYVQPNEEEQ GLTIGTYHLK VKVPVEGQYG
     LYIRTIRQSN RVFMNDIEVG GKGNPSETLS GYQAENDDKY TVFTQSRNNI LDIVIHVTGF
     HHPQAGIIYP IEFGTMQAIQ HHYRIKVLTD VLVSVGYVIF GIIYIMSYIQ NRRRKEELFF
     GLFAILLGLY MSFINQKVFF MIVPITHALG QLRLQLGSVP LVIMCLTLFI YYMYPQLTKK
     RTLYALLVLM GITFFMYAIY NPFTHNTRAT SEEEVTFRKL VYIALNAPVV AYNVWVLIRV
     LLKRLEGARY ILIVLIAICC YSVLLAINFI TDIPFDYSEI LLFLLMLFGF VLLLNYRANV
     AFIKIQALSE ELLTHNQMKD EFLLKTSHEL RTPLNGIVNL SKSLMEGAQG PLKRAQQEQV
     ILIHNITQRL GHLVEDLLFS STHMTGEIRV SPRAVPITVI NEVMTEIQNI MPKNSHVRLI
     TEVDKALPNM LTDELRFKQV LYNLLHNAIQ HTKIGEIIVT AHAQQSQMVI RVSDTGAGIP
     TQDIEHIFTA FYQVKKQGQK EGLGLGLSIA KNIVEKLDGA IYVTSSLGEG TTFTFTMPLA
     TETLVNNEQI FTTMGTQAAT EVLKLNLPLF YKGNDKKILV VDDDHVNIKV LADNLALKGY
     TVIAVDNGFD AVAYLKTNEV DCLLIDLMMN GMSGYELCKQ VRKQYDMLEL PIIVLTAIMK
     HSDLVLTLQV GANDYLQKPV SMDELLIRIE SLLAVRQSSI DAIEVEMNYL YAQVTPHFVY
     NTLNTIIGLS YTNMNDTREA LYCLATYFRA KLNVHYRNSM VPIEEEIELV KAYLYIEKMR
     FVDRLTINYD IDESIQLMIP ALSIQPLVEN AVVHGISKKL EGGTIEISVQ RDGQFIRIKI
     YDNGVGIPDE KLQQLLNGEG SRIGFMNPLK KFKLMKNASL RLYSEVGKGT TILILLPEGD
     GA
//
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