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Database: UniProt
Entry: A2SDJ3_METPP
LinkDB: A2SDJ3_METPP
Original site: A2SDJ3_METPP 
ID   A2SDJ3_METPP            Unreviewed;      1170 AA.
AC   A2SDJ3;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=Mpe_A0670 {ECO:0000313|EMBL:ABM93632.1};
OS   Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Methylibium.
OX   NCBI_TaxID=420662 {ECO:0000313|EMBL:ABM93632.1, ECO:0000313|Proteomes:UP000000366};
RN   [1] {ECO:0000313|EMBL:ABM93632.1, ECO:0000313|Proteomes:UP000000366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1232 / LMG 22953 / PM1
RC   {ECO:0000313|Proteomes:UP000000366};
RX   PubMed=17158667; DOI=10.1128/JB.01259-06;
RA   Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA   Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA   Hristova K.R.;
RT   "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT   proteobacterium Methylibium petroleiphilum PM1.";
RL   J. Bacteriol. 189:1931-1945(2007).
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};
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DR   EMBL; CP000555; ABM93632.1; -; Genomic_DNA.
DR   RefSeq; WP_011828270.1; NC_008825.1.
DR   AlphaFoldDB; A2SDJ3; -.
DR   STRING; 420662.Mpe_A0670; -.
DR   KEGG; mpt:Mpe_A0670; -.
DR   eggNOG; COG0784; Bacteria.
DR   eggNOG; COG1457; Bacteria.
DR   eggNOG; COG2205; Bacteria.
DR   HOGENOM; CLU_008084_1_0_4; -.
DR   Proteomes; UP000000366; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
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; 1.
DR   Gene3D; 1.10.4160.10; Hydantoin permease; 1.
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; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
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   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ABM93632.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000000366};
KW   Transferase {ECO:0000313|EMBL:ABM93632.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        59..83
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        89..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        124..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        167..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        193..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        232..252
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        273..306
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        326..343
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        375..397
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        403..421
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        442..465
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        471..491
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        590..610
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        630..654
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          715..929
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          953..1069
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          681..708
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         1003
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1170 AA;  126379 MW;  00C2170D389DD12F CRC64;
     MPSHPAALPP ASDTPPAAPV QRVIKLRRDY NSWVARETME DYALRFTPRA FRKWSAWRVA
     NTAIGGAASF LVLEAVGATL LVQHGFVNAA LAILVTGLVI FLAGLPVSVY AARHGVDMDL
     LTRGAGFGYI GSTLTSLIYA SFTFIFFALE AAVMAYALEL AFDIPPAWGY LICAVVVIPL
     VTHGVTAISR LQVWTQPLWL AMLVAPYVYV FAENPGVVDG LLAYGGEKGV AGFSWLHFGA
     ATTVGIALIT QMGEQADYLR FMPEKRAGQR GRWWLGVLVG GPGWVLPGVL KMLGGTLLAW
     LAISHMVPLD RAVDPNQMYL AAYEHVFPHY GLAVAATALF VVISQLKINV TNAYAGSLAW
     SNFFARLTHS HPGRVVWMVF NTAIALMLME LNVFQAIGSV LGLYSNVAIA WMMAVVADLV
     VNKPLGLSPP GIEFRRAHLY DVNPVGVGAM GIASLLSITA HIGLYGPMAQ AWSAAIAMVT
     AFAAAPLIAW ATKGRYYIAR QPEPLAAGDD GRYPRLSRCC ICEREYERDD IASCPAYGGP
     ICSLCCTLDA RCGDLCKPPE AKLAAQWSAA LRRLLPRAVW PYIDTGLGHY LLLMLTVVPL
     LGGLFALLYH QELRTLAASG APLAPAVAGA LKLGFVKAFA ALLLIAGTVA WWLVLTHKSR
     EVAQEESNRQ TAALRTEIES HRRTDAQLQE AKLQAERAMH QAEQANRAKS RYITAISHEL
     RTPLNSILGY AQLLEEDEAM PPHRAQAVRV IRRGGDHLAS LIEDTLDLAR IESGKLALEV
     RPLRLCEAVQ ELARMFELQA RAKGLVFRHE IEGPDVVRAD EKRLRQILIN LLGNAVKFTA
     QGEVVFRMRY AREIAHFEIE DSGPGMTSDE LARVFEPFER GGALAGGGHG TGIGLTIAKM
     LTDLMGGEMT VRSTPGRGTA FAIRLFLPQA SEATVAPAVR VARRIGYAGA RRSVLVVDNE
     EADRGLLATV LEPLGFAVRQ AASGEAALRL LRAGPPPDAI LMDLAMPGLD GWATIRQLRE
     EGLCEAPVAI VSANAFDRGL DNDVGVTPAD FFVKPVRVTD LLQWLGQRLA LEWIDAPPRH
     ATASGPPALA TPAGPLPVAA FARRAALDEL ARLGYLRGLL GELSAIEAED PAAAAWTGPV
     RELAQQFRFD AIRALLNPRD EEPEDAAAAA
//
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