ID L0MCL1_9GAMM Unreviewed; 510 AA.
AC L0MCL1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Signal transduction histidine kinase, glucose-6-phosphate specific {ECO:0000313|EMBL:AGB80495.1};
GN ORFNames=D781_0099 {ECO:0000313|EMBL:AGB80495.1};
OS Serratia sp. FGI94.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=671990 {ECO:0000313|EMBL:AGB80495.1, ECO:0000313|Proteomes:UP000011001};
RN [1] {ECO:0000313|EMBL:AGB80495.1, ECO:0000313|Proteomes:UP000011001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGI94 {ECO:0000313|EMBL:AGB80495.1,
RC ECO:0000313|Proteomes:UP000011001};
RX PubMed=23516234;
RA Aylward F.O., Tremmel D.M., Starrett G.J., Bruce D.C., Chain P., Chen A.,
RA Davenport K.W., Detter C., Han C.S., Han J., Huntemann M., Ivanova N.N.,
RA Kyrpides N.C., Markowitz V., Mavrommatis K., Nolan M., Pagani I., Pati A.,
RA Pitluck S., Teshima H., Deshpande S., Goodwin L., Woyke T., Currie C.R.;
RT "Complete Genome of Serratia sp. Strain FGI 94, a Strain Associated with
RT Leaf-Cutter Ant Fungus Gardens.";
RL Genome Announc. 1:E0023912-E0023912(2013).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP003942; AGB80495.1; -; Genomic_DNA.
DR RefSeq; WP_015344091.1; NC_020064.1.
DR AlphaFoldDB; L0MCL1; -.
DR KEGG; smaf:D781_0099; -.
DR PATRIC; fig|1249634.3.peg.91; -.
DR eggNOG; COG3851; Bacteria.
DR HOGENOM; CLU_041023_0_0_6; -.
DR OrthoDB; 9797605at2; -.
DR Proteomes; UP000011001; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR CDD; cd16917; HATPase_UhpB-NarQ-NarX-like; 1.
DR Gene3D; 1.20.5.1930; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR007895; MASE1.
DR InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR PANTHER; PTHR24421; NITRATE/NITRITE SENSOR PROTEIN NARX-RELATED; 1.
DR PANTHER; PTHR24421:SF37; SIGNAL TRANSDUCTION HISTIDINE-PROTEIN KINASE_PHOSPHATASE UHPB; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF07730; HisKA_3; 1.
DR Pfam; PF05231; MASE1; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AGB80495.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 7..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 52..69
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 76..99
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 111..132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 139..161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 181..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 210..228
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 409..504
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
SQ SEQUENCE 510 AA; 56473 MW; 7F1941EBB078E6C7 CRC64;
MIAGAALFFI YAASVFCLWG IGAALIDPPW QALLLFPFGL RMGILLQSPR RYWPGILLAD
VLLILLLADQ FGATRALWAS LTVLALTVLL SCAASPWLLR HQQSDSEWRW PLQQGAVLAL
AAVLQAAVWQ LFSGDGARAL LLGLTGGFTI APTCLLLWHY LARQIWVPLE PGLIHKPVRL
RLRHLAMYLL LFALSIWLQQ QVNVAELRRF APFCLAIPIV FMAYRYGWQG ALLATLLNGV
VLMAGEPPRP DAHRDLLLSL LAQSLTGLLL GAGIQRQREL NQQLRRRLAE NRQLARALVT
AEERTRREVA RELHDEVGQN VTVIRTQASI VKRLAPQPQV QTCADTIDAL ALRVYDGVHD
VLAQLWPAAL NNLPLSAAVA AMLRDQLPQD DSVTGVLLWQ VPEPALDDTL KITLYRICQE
GVTNVRRHAD ASRIELTARL HTPADGQAQV ELTLRDNGVG IDLARHEPGY GLRGMRERVS
ALGGTLRLTV EQGLCLHVIL PTVSPEKRQN
//
