ID C5B4Z3_METEA Unreviewed; 1072 AA.
AC C5B4Z3;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=MexAM1_META2p0678 {ECO:0000313|EMBL:ACS43525.1};
OS Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB
OS 9133 / AM1) (Methylobacterium extorquens).
OG Plasmid megaplasmid {ECO:0000313|EMBL:ACS43525.1,
OG ECO:0000313|Proteomes:UP000009081}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
OX NCBI_TaxID=272630 {ECO:0000313|EMBL:ACS43525.1, ECO:0000313|Proteomes:UP000009081};
RN [1] {ECO:0000313|EMBL:ACS43525.1, ECO:0000313|Proteomes:UP000009081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
RC {ECO:0000313|Proteomes:UP000009081};
RX PubMed=19440302; DOI=10.1371/journal.pone.0005584;
RA Vuilleumier S., Chistoserdova L., Lee M.-C., Bringel F., Lajus A., Zhou Y.,
RA Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., Gillett W.,
RA Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., Muller E.,
RA Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., Roche D.,
RA Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., Marx C.J.,
RA Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., Medigue C.,
RA Lidstrom M.E.;
RT "Methylobacterium genome sequences: a reference blueprint to investigate
RT microbial metabolism of C1 compounds from natural and industrial sources.";
RL PLoS ONE 4:E5584-E5584(2009).
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 -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP001511; ACS43525.1; -; Genomic_DNA.
DR RefSeq; WP_012753975.1; NC_012811.1.
DR AlphaFoldDB; C5B4Z3; -.
DR KEGG; mea:Mex_2p0678; -.
DR HOGENOM; CLU_000445_114_15_5; -.
DR OrthoDB; 9789782at2; -.
DR Proteomes; UP000009081; Plasmid megaplasmid.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00088; HPT; 1.
DR CDD; cd00130; PAS; 2.
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; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.30.450.20; PAS 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; IPR036641; HPT_dom_sf.
DR InterPro; IPR007895; MASE1.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF05231; MASE1; 1.
DR Pfam; PF08448; PAS_4; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000313|EMBL:ACS43525.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Plasmid {ECO:0000313|EMBL:ACS43525.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009081};
KW Transferase {ECO:0000313|EMBL:ACS43525.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 29..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 138..159
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 171..193
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 245..264
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 284..305
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 338..391
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 447..517
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 521..573
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 591..813
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 834..951
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 978..1072
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 883
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1017
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1072 AA; 116654 MW; EFF5B877B1BFD88E CRC64;
MTAPSDPSRD RALPFTPGAD LRHTAPSEFF LPFLLGVFVL FTAWLGIMNQ QEGRIAQIWL
PNPVLYVVLM RASWGRWPVY LGVATSANFL ADLLAGDSPW LAAGLTFANI SEVVLAVAPL
KRWFSEGLDL TRLRHLRAFV FVSTLAAPAI SATVAAAVIL LHNGSPYGWT WLIWASADGL
SLLVLVPLIY VLLEWRRGPI LEDRWLEAVL WTALLGATLF ATFKLAPYPL LFLPILVLVY
MSARIGPSGL LLGIVPTAVA AFAYTQAGIG PIAQSGLGRQ EQILLLEGFL AASVLAVLPV
VAMLADKARL EKSLNEAKAL FLGVFDSSPE MLIVQYQDAE GQIRVETCNE NAAQAFGRSQ
EACIGRTVES LIRGKASRNV AEDIEHVMRT GESVRRTREV RHRERGTIFE DISVPLRDPS
TGRVTRVLSS VRDITARLQA EKAVRVSEAR LRLLAENTTD MIVEFDLGLR CTYVSPASRE
IIGFAPAELV GTDPYEHCLQ DDAPEIQRAV APLIDGTFSH AASTHRALHR DGRTVWIETR
WSLVRSESGR PAGVVASMRD VTERKQAEIA LVRAQAEAEQ ASAAKSDFLA TMSHEIRTPL
NGIAGYAGLL MTEDGLPARS RRHVERIQTA SQVLKTVVDD VLDFSKIEAG RVELVPTTFG
LARLVDDVVA IVRGGVPADG PHVEGEIAPS LDGAYVGDEN RLRQILLNLL NNAVKFTPAG
SVDLRIVDLG LEAGSRRLRF SVRDTGIGIS PEQQKLLFRK FSQIDASNVR RYGGTGLGLA
ISQRLVGLMG GAIEVSSSLG TGSEFSFEIS LPEHADAPPQ VETVRLDVGS CSCRILVVED
LEANRELVVS ILSAAGHETE AVVDGVEAVE KAERGGFDLI LMDIQMPRMD GIAAARRIRE
LPGPAGEVPI VAMTANVLPS QVAAIREAGM DDHVGKPFEI QALERTVARW VCGRAQIAPE
APPAAPLWEH ETAYRALVAS IGSENSRRVF EGFEQELRRR FQDVGRTDRA GLARDAHAIR
GEAGQLGFPD LAQACRELED ACESGGRVER PMERVDIERR RALEAIALLR AA
//
