ID E8TMM9_MESCW Unreviewed; 773 AA.
AC E8TMM9;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Mesci_4866 {ECO:0000313|EMBL:ADV13974.1};
OS Mesorhizobium ciceri biovar biserrulae (strain HAMBI 2942 / LMG 23838 /
OS WSM1271).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=765698 {ECO:0000313|EMBL:ADV13974.1, ECO:0000313|Proteomes:UP000007471};
RN [1] {ECO:0000313|Proteomes:UP000007471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HAMBI 2942 / LMG 23838 / WSM1271
RC {ECO:0000313|Proteomes:UP000007471};
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Nandasena K., Reeve W.G., Howieson J.G., O'Hara G.,
RA Tiwari R.P., Woyke T.;
RT "Complete sequence of chromosome of Mesorhizobium ciceri bv. biserrulae
RT WSM1271.";
RL Submitted (JAN-2011) 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};
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DR EMBL; CP002447; ADV13974.1; -; Genomic_DNA.
DR RefSeq; WP_013532627.1; NC_014923.1.
DR RefSeq; YP_004144024.1; NC_014923.1.
DR AlphaFoldDB; E8TMM9; -.
DR STRING; 765698.Mesci_4866; -.
DR KEGG; mci:Mesci_4866; -.
DR PATRIC; fig|765698.3.peg.5381; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_114_71_5; -.
DR OrthoDB; 9801651at2; -.
DR Proteomes; UP000007471; Chromosome.
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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF12860; PAS_7; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 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; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000313|EMBL:ADV13974.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000313|EMBL:ADV13974.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 50..69
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 210..232
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 273..305
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 323..374
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 545..764
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 773 AA; 84875 MW; F6E571E7114E0FEA CRC64;
MAKADAWGAP GGTVFAHRET RGDGLAGNTR LIAEPAYRRL LAAEPLLRRS IPVLIITFLI
VIAALRVLSL MNERDDVERN AKAILTLAAG QLASSLATTS ETVPGAIQDL LETTSRQGAM
GRSHVLVITD SAFKIVAVTP RSMPWQGHSL DGLVEGGQPL FMFGDRAGVM DVNIDGRDWY
AAVSLANGGK GASAALVPQD AVFDAWRKTV SLNVTLFVLT AGVLIVILYA YFGQAARAQA
ADRIYLEAHQ RIDMALVRGR CGLWDWDMVR GKMYWSRSMY DMLGYKPCET MLSFGEVDQI
IHPEDGDLFE LANRIVAREI DHIDQVFRMR HADGQWVWMR ARAQVIDPEA PEIQLIGIAV
DVTEQRHLAL RSEAADLRLR TAIENINESF VLWDSTQHLI MCNSKYQQDN GLSDRDVMPG
TARAALEERM LAFASERRLA HTSGLQGGAT FERQLADGRW LQVNELKTRD GGIVSVGSDI
TQIKLHQEKL VDSERRLMAT IHDLSLARRA EEERSRELVD LNRKYMKETE RAEAANRAKS
EFLANMSHEL RTPLNAIIGF SELMEQGLFG PLGSERYEEY ATDINSSGKY LLGVINDILD
MSKIEAGQFS LDREEIDLGP LISETVRVVS LQAAQKAISV ETRIADALTL VADRRAIKQI
VINLLSNAVK FTGHGGHISV RARNTSGALV LTIEDNGCGI PKEALGKLGR PFEQVQNQFS
KSHAGSGLGL AISRSLAELQ GGALKIRSSE GVGTIVSVRI PVKKSVLAVK VAA
//
