ID A0A1E7JLT1_9ACTN Unreviewed; 531 AA.
AC A0A1E7JLT1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AN215_17515 {ECO:0000313|EMBL:OEU88603.1};
OS Streptomyces abyssalis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=933944 {ECO:0000313|EMBL:OEU88603.1, ECO:0000313|Proteomes:UP000176087};
RN [1] {ECO:0000313|EMBL:OEU88603.1, ECO:0000313|Proteomes:UP000176087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCSIO 10390 {ECO:0000313|EMBL:OEU88603.1,
RC ECO:0000313|Proteomes:UP000176087};
RX PubMed=27446038; DOI=10.3389/fmicb.2016.00998;
RA Tian X., Zhang Z., Yang T., Chen M., Li J., Chen F., Yang J., Li W.,
RA Zhang B., Zhang Z., Wu J., Zhang C., Long L., Xiao J.;
RT "Comparative Genomics Analysis of Streptomyces Species Reveals Their
RT Adaptation to the Marine Environment and Their Diversity at the Genomic
RT Level.";
RL Front. Microbiol. 7:998-998(2016).
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 -!- 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:OEU88603.1}.
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DR EMBL; LJGT01000040; OEU88603.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E7JLT1; -.
DR STRING; 933944.AN215_17515; -.
DR PATRIC; fig|933944.5.peg.2798; -.
DR OrthoDB; 9786919at2; -.
DR Proteomes; UP000176087; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
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 PANTHER; PTHR45436:SF5; SENSOR HISTIDINE KINASE TRCS; 1.
DR PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 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 PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OEU88603.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000176087};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 180..242
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 257..505
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 62..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 531 AA; 55495 MW; DF10E6739F54D020 CRC64;
MLIAVVCAVI GTVTAIAVNS SLESRLDDEL RASVQRSYGP PGASVPRPDD MRFVAVPGQP
IGTVGARTGD DGGLTGTARS TDLSGGPAMD LSDRLARLTA EQSRALEKVP RDGRPHTVSL
PELGDYRVQS GAPPGEEAGL LVGLPMSGVQ STLKTLVVVE VCVSAAGLVA AGIAGAATVR
IALRPLRRVA ATATKVTRLP LHSGDVELPH RVSERDTDPR TEVGQVGAAL NSMLGHVGAA
LEARQESETR VRQFVADASH ELRTPLASIR GYAELTRRVS RDPRRPGKDA GTSGRDAGSS
ADGGAQETVP PWGPDALHAL DRIEAEAARM SGLVEDLLLL ARLDAGRPLE REPVSLSSLV
VDAVSDARAA GPRHLWRLEL PAEPVEVPGD GMRLQQVLGN LLANARTHTP PGSTVTARVR
SEPEGREGRQ VVVEVEDDGP GIPADVLPHV FERFARGDAT RSRAHGSTGL GLAIVEAVVT
AHHGRVSADS APGSTVFAVR FPSAAHAAHA EQPEQASRSD SQPTQRLSTP S
//
