ID D3RN99_ALLVD Unreviewed; 778 AA.
AC D3RN99;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Alvin_0424 {ECO:0000313|EMBL:ADC61383.1};
OS Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB
OS 10441 / D) (Chromatium vinosum).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Allochromatium.
OX NCBI_TaxID=572477 {ECO:0000313|EMBL:ADC61383.1, ECO:0000313|Proteomes:UP000001441};
RN [1] {ECO:0000313|EMBL:ADC61383.1, ECO:0000313|Proteomes:UP000001441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D
RC {ECO:0000313|Proteomes:UP000001441};
RX PubMed=22675582; DOI=10.4056/sigs.2335270;
RA Weissgerber T., Zigann R., Bruce D., Chang Y.J., Detter J.C., Han C.,
RA Hauser L., Jeffries C.D., Land M., Munk A.C., Tapia R., Dahl C.;
RT "Complete genome sequence of Allochromatium vinosum DSM 180(T).";
RL Stand. Genomic Sci. 5:311-330(2011).
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; CP001896; ADC61383.1; -; Genomic_DNA.
DR RefSeq; WP_012969659.1; NC_013851.1.
DR AlphaFoldDB; D3RN99; -.
DR STRING; 572477.Alvin_0424; -.
DR KEGG; alv:Alvin_0424; -.
DR eggNOG; COG0642; Bacteria.
DR eggNOG; COG0784; Bacteria.
DR HOGENOM; CLU_000445_104_15_6; -.
DR OrthoDB; 5563233at2; -.
DR Proteomes; UP000001441; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
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; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR033417; CHASE8.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF6; RESPONSE REGULATORY DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF17152; CHASE8; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
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; SSF158472; HAMP domain-like; 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; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ADC61383.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000001441};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 174..196
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 201..254
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 276..497
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 651..769
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 700
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 778 AA; 85956 MW; 4756E4A22E5D2A32 CRC64;
MMTRFSRLSM RDKVIAVVML VSALVLLVLA LLVVIADIIE RRGALVERVG ALTRVASIST
SAALAFQDAP GAEEILAALG TEAEIIGIEI RDLDRVSFAR YRSPHPHHRT LQKRIEISEQ
REREAGDAPW PSDTQPNARF QRGYLDVHMT VQIDGRPLGY MDLQYDTTDL TRRIWLQVWL
ALVVFAGGLG LAFLLASRLH RLISEPIARV AVAMERITLD EDYGVRLGSI GTDELATLTR
AFDAMLERIE QRDAELREAR DAAERANRAK SHFLANMSHE IRTPMNGIIG MTELLQETDL
NAAQRDCTRV IQDSAAALMR IINDILDMSR IEAGRLELER LDFDPRESIE RTLEPLREIA
QRKGLEFAIE LDPELPARLR GDPGRLRQIL TNLVSNAIKF TEQGRVSVTL DCLERTDDWV
RFVIAVRDTG IGLSTEECSR LFERFSQADV STRRRYGGTG LGLAISRQLV ELMGGGIDVE
SKPGLGSVFR VELVLESSES PPAVDRRLAG LQTLVLVQEP SLAAQLGGML EDLGMSVEHQ
TSLAAAIESA LTRAARGQTF DVLLLEHEQL PAPTSPAGSL LHEMSARALA VLRLRARGGA
AGDDPVWGRL PEIGLPPTHV ELQNGLSAII RSRGAGGHGE GAKQRPSLGL RVLVAEDNPA
NQRVIEWMLT ALDCEVELHP NGRSLLESFT ARPADLVLMD CQMPVMDGYE TTRRLRKLES
ALGRRVPIIA VTAQAMAGDR ERVIAAGMDD HLSKPFTLEA LATLLTRWKT ERTWISSE
//
