ID A0A1V0GZN8_9RHOB Unreviewed; 937 AA.
AC A0A1V0GZN8;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 2.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=A6J80_23105 {ECO:0000313|EMBL:ARC39159.2};
OS Paracoccus yeei.
OG Plasmid unnamed7 {ECO:0000313|EMBL:ARC39159.2,
OG ECO:0000313|Proteomes:UP000191257}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=147645 {ECO:0000313|EMBL:ARC39159.2, ECO:0000313|Proteomes:UP000191257};
RN [1] {ECO:0000313|Proteomes:UP000191257}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FDAARGOS_252 {ECO:0000313|Proteomes:UP000191257};
RC PLASMID=Plasmid unnamed7 {ECO:0000313|Proteomes:UP000191257};
RA Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Tallon L.,
RA Sadzewicz L., Sengamalay N., Ott S., Godinez A., Nagaraj S., Nadendla S.,
RA Geyer C., Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (MAR-2017) 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};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP020447; ARC39159.2; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V0GZN8; -.
DR KEGG; pye:A6J80_23105; -.
DR Proteomes; UP000191257; Plasmid unnamed7.
DR GO; GO:0016020; C: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; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR CDD; cd16172; TorS_sensor_domain; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 1.20.58.920; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 6.10.340.10; -; 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 InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003660; HAMP_dom.
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; IPR037952; Sensor_TorS.
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 InterPro; IPR038188; TorS_sensor_sf.
DR PANTHER; PTHR43047:SF79; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF21689; TorS_sensor_domain; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF47162; Apolipoprotein; 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 PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Plasmid {ECO:0000313|EMBL:ARC39159.2};
KW Reference proteome {ECO:0000313|Proteomes:UP000191257};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 341..363
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 365..417
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 474..692
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 709..827
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 840..935
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 410..446
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 758
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 879
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 937 AA; 100218 MW; BE382B1B7B6F9732 CRC64;
MGRFGRKSRL GWQLLLAFVV IAGAPGLMGL LGWLELRDLA DRQSRLIAQT IPAIAEVRGF
AEESSRVVAI APDLAAVTDD HVRRERAAFL FGQVDALRDR IRRYESSGQP IPAPLSRSEA
EVRQGIARLD LLVQRRLAAE ADQRRRLDEG LAATTELLEI TDTLAANAEV AVSAGVVSLY
DLWDRRAALA ERLDRLVEVD LFQLGQMFEL RGHVAEIALL LNRIGETRRE PELERLRGAL
VARLGVVTRR LAMVPDRSRA ERALVLLHAI TPAAASPPGT EDFPGLTARL IALDAQTTAA
QAELRDAALR LDTQAAALAD GIVGRATRAG EAAQAAIRRT LIASAIGSLL PLMVSAGVVW
FYVRGKITRR LDALAARMGG LRAGELHEQV VPRGEDEIAR MEQAVEVFRL QALENRALAA
ERDRNLEELR RHREELRQLV DEQTERLRGE VAAHAEARAR AEAADRAKSQ FLAMMSHEIR
TPMHGVLGLL HGLMQDDLAG RARERVVVAL ASGEGLMALL NTLLDDAKAL DGAVVLRQAA
FDPAALLRET AALMAGSAEG KGLWLRVDAP DCGWLIGDAA RLRQVLFNLL ANAIRFTVTG
GVTLRLRARA GPGGVLLVME VADTGKGIAP EAQRRIFGLF EQEDAETARR YGGTGLGLAI
SRRLTGAMGG RLSVKSAPGQ GARFRFAAHF PAAAAPVQPA APEAAGSLHL LVVEDHPVNR
MVLDGYLSGL GHGFEMVDCA EAALARLAQA RFDAVLMDVN LPGMSGIEAA RRIRQSAPDG
AGAVPVIGIS AHVQPEERAA CQAAGMVEVL SKPLAPAELR RALAGLRAAG VLAPALADLP
APQVARLARL YLDGMARDMA AIRAALAQGD AGAAARAAHR WRGASGNFGL SDLVAALARF
ERALAEGPGA APLWPNLAAL AEERAAQMQR ELARLPA
//
