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Database: UniProt
Entry: Q1YKL4_AURMS
LinkDB: Q1YKL4_AURMS
Original site: Q1YKL4_AURMS 
ID   Q1YKL4_AURMS            Unreviewed;       669 AA.
AC   Q1YKL4;
DT   02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   02-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SI859A1_00629 {ECO:0000313|EMBL:EAS50509.1};
OS   Aurantimonas manganoxydans (strain ATCC BAA-1229 / DSM 21871 / SI85-9A1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Aurantimonadaceae; Aurantimonas.
OX   NCBI_TaxID=287752 {ECO:0000313|EMBL:EAS50509.1, ECO:0000313|Proteomes:UP000000321};
RN   [1] {ECO:0000313|EMBL:EAS50509.1, ECO:0000313|Proteomes:UP000000321}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SI85-9A1 {ECO:0000313|EMBL:EAS50509.1,
RC   ECO:0000313|Proteomes:UP000000321};
RX   PubMed=18344346; DOI=10.1128/AEM.01656-07;
RA   Dick G.J., Podell S., Johnson H.A., Rivera-Espinoza Y., Bernier-Latmani R.,
RA   McCarthy J.K., Torpey J.W., Clement B.G., Gaasterland T., Tebo B.M.;
RT   "Genomic insights into Mn(II) oxidation by the marine alphaproteobacterium
RT   Aurantimonas sp. strain SI85-9A1.";
RL   Appl. Environ. Microbiol. 74:2646-2658(2008).
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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:EAS50509.1}.
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DR   EMBL; AAPJ01000002; EAS50509.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1YKL4; -.
DR   HOGENOM; CLU_410393_0_0_5; -.
DR   BioCyc; AURANTIMONAS:SI859A1_00629-MONOMER; -.
DR   Proteomes; UP000000321; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004673; F:protein histidine kinase activity; IEA:InterPro.
DR   CDD; cd12913; PDC1_MCP_like; 1.
DR   Gene3D; 6.10.340.10; -; 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; IPR033479; dCache_1.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR029151; Sensor-like_sf.
DR   InterPro; IPR011102; Sig_transdc_His_kinase_HWE.
DR   PANTHER; PTHR41523:SF7; ETHYLENE RESPONSE SENSOR PROTEIN; 1.
DR   PANTHER; PTHR41523; TWO-COMPONENT SYSTEM SENSOR PROTEIN; 1.
DR   Pfam; PF02743; dCache_1; 1.
DR   Pfam; PF07536; HWE_HK; 1.
DR   SMART; SM00911; HWE_HK; 1.
DR   SUPFAM; SSF103190; Sensory domain-like; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EAS50509.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000321};
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}.
FT   TRANSMEM        349..369
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          470..550
FT                   /note="Signal transduction histidine kinase HWE region"
FT                   /evidence="ECO:0000259|SMART:SM00911"
FT   COILED          418..460
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   669 AA;  72816 MW;  9A844FDB03C9DDFA CRC64;
     MGWGGQGGMW SFRTVLTSTL VALQVVALLA ILALTYFASQ SVLLSYAEQL TQRVADDTTT
     FTQNFLNPAD DAAALSQRLA ESPVLGTADR PALERYFYEI LRSRIDFAGI FYGAADGSFI
     YVSRDTTVEG AQYRMKRIAT QPTRTVELVY LTEDLRPVSR RRDDADTYDP RTRPWYVKAS
     MSRDVVWTDP YIFFSSQRPG ITVATPVRAD DRLGMRGAVG IDIEIHALSK FLDGLRIGER
     GSAAIVSQSG EVIAHRDSSF LLAEDVSGGQ RFARVWEIDD PALAQAVSTL PGGLANVKPG
     ETRLTRFEAG GENWRGAVKR LAGSRTPWAV VTYLPESDIL GPIYSVRNIG IAVVAGVAAL
     TALLGVLLAR ALTRPIGALA CQAERISEGD FGDIPLPSMW TKELAGTRQA MRRATSWLRD
     YRRENETLTE QLREAGRVLE RRVEERTEEL EVANRGLEKA HGNAEMLTHE LDHRVKNLFA
     ITASLVTLAA KHAATPMEAA DEARGRINAL ARAHADTQSA RETQLAGIVT SVLKPYAGID
     EVKLTIEGDP VTVSSSSVTP LGLILYELAT NAAKYGALRG SGGVLEVRWS AAGDGSVRMV
     WAETPTEPPT GDELHQAQHT GFGSVMLDAM ASRLNAGIQR QISPEGLRVI LTMEKLEEHA
     GPRPTSVDA
//
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