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Database: UniProt
Entry: A0A177HLN9_9ACTN
LinkDB: A0A177HLN9_9ACTN
Original site: A0A177HLN9_9ACTN 
ID   A0A177HLN9_9ACTN        Unreviewed;       523 AA.
AC   A0A177HLN9;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   Name=tcrY_5 {ECO:0000313|EMBL:OAH11480.1};
GN   ORFNames=STSP_51530 {ECO:0000313|EMBL:OAH11480.1};
OS   Streptomyces jeddahensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1716141 {ECO:0000313|EMBL:OAH11480.1, ECO:0000313|Proteomes:UP000077381};
RN   [1] {ECO:0000313|EMBL:OAH11480.1, ECO:0000313|Proteomes:UP000077381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G25(2015) {ECO:0000313|Proteomes:UP000077381};
RA   Poehlein A., Roettig A., Hiessl S., Hauschild P., Schauer J., Madkour M.H.,
RA   Al-Ansari A.M., Almakishah N.H., Steinbuechel A., Daniel R.;
RT   "Genome sequence of Streptomyces sp. G25.";
RL   Submitted (DEC-2015) 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: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
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:OAH11480.1}.
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DR   EMBL; LOHS01000108; OAH11480.1; -; Genomic_DNA.
DR   RefSeq; WP_067282497.1; NZ_LOHS01000108.1.
DR   AlphaFoldDB; A0A177HLN9; -.
DR   STRING; 1716141.STSP_51530; -.
DR   PATRIC; fig|1716141.3.peg.5416; -.
DR   OrthoDB; 9786919at2; -.
DR   Proteomes; UP000077381; Unassembled WGS sequence.
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; 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; 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.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OAH11480.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077381};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OAH11480.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        167..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          191..244
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          259..509
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   523 AA;  55766 MW;  A608271DCF67EEEE CRC64;
     MRRWLRRLKP RSLRARLVLG VTLLATSAVL LCQAAGLALL HSWLTDQVDG RLTRFQPVPQ
     LYQDVADGRT ASGEAGRTSG LPSDYRVYFY DRGGHRLAMS LSGDGGSAGP RLPKSEAELG
     LKNGRPATVA ATDGGSTWRV IARSGTDGTR VVVALPLKEV DEATSRMLWF SLAIGVAVAA
     GVVLFGTLAV RLGLRPLVGV ERTARRIAEG ELELSVPDRH AVTEVGHLSR ALNTMLDRLR
     TALRRTEASE QRLRHFLADA GHELRTPLTS LQGFAELLVQ EPEMSLERRQ EAQQLIVRNA
     DRMSRLIESL SQLARLGEVP ATRWQPVDLL SLVADGIAAV AVRHPGRSIG LGTLADPEDD
     ARVNELDVVE AVGDPHQLAQ ILSNLLTNAC VHTPTGTHIQ VRVGTFRVRP HGPGTTGPGR
     TSANAPLIPG TRVCAVEVAD DGAGLAESHA RRVFERFYRA DAAERAAAAG SGLGLAIAAG
     AAEANGGRLE LEARPGEGCT FRLLLPYQPA AAATAAPAPH TCV
//
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