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Database: UniProt
Entry: U5W041_9ACTN
LinkDB: U5W041_9ACTN
Original site: U5W041_9ACTN 
ID   U5W041_9ACTN            Unreviewed;       593 AA.
AC   U5W041;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=AFR_21160 {ECO:0000313|EMBL:AGZ42504.1};
OS   Actinoplanes friuliensis DSM 7358.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=1246995 {ECO:0000313|EMBL:AGZ42504.1, ECO:0000313|Proteomes:UP000017746};
RN   [1] {ECO:0000313|EMBL:AGZ42504.1, ECO:0000313|Proteomes:UP000017746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7358 {ECO:0000313|EMBL:AGZ42504.1,
RC   ECO:0000313|Proteomes:UP000017746};
RX   PubMed=24637369; DOI=10.1016/j.jbiotec.2014.03.011;
RA   Ruckert C., Szczepanowski R., Albersmeier A., Goesmann A., Fischer N.,
RA   Steinkamper A., Puhler A., Biener R., Schwartz D., Kalinowski J.;
RT   "Complete genome sequence of the actinobacterium Actinoplanes friuliensis
RT   HAG 010964, producer of the lipopeptide antibiotic friulimycin.";
RL   J. Biotechnol. 178:41-42(2014).
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; CP006272; AGZ42504.1; -; Genomic_DNA.
DR   RefSeq; WP_023362876.1; NC_022657.1.
DR   AlphaFoldDB; U5W041; -.
DR   STRING; 1246995.AFR_21160; -.
DR   KEGG; afs:AFR_21160; -.
DR   PATRIC; fig|1246995.3.peg.4289; -.
DR   eggNOG; COG2770; Bacteria.
DR   eggNOG; COG5002; Bacteria.
DR   HOGENOM; CLU_000445_89_6_11; -.
DR   OrthoDB; 9786919at2; -.
DR   Proteomes; UP000017746; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
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:AGZ42504.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017746};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   DOMAIN          310..362
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          370..584
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   593 AA;  63329 MW;  E7F19A7BFD8D2C35 CRC64;
     MSFRLRIFLL VVAVAVTAIG ATAWLTLSLT SREVTRAQES SEKHATEIRD AIERYGVTHG
     RWNGLDTLVR ELSERTGLHI QVSTTPSDQP IVDSDNLAGR ASGPLQAVPI SVEPRPKLSI
     SNALFADSKS ADIMFLKLNG RISPDTPIAP RNLFGAEPRD PYRGSPIALM LRQLAQYRAG
     LVAVRCIADE NPGQPDALAL DSAPYLSKAQ ITTYSACVKR ASVKVLEDTA WLADNWRTFA
     ACATTQGALG REGCMTATFF DGAGSTSAVA VEVFLGAPTG AAIEDLGRPA VLGAAGLIVV
     ALIGTAWIAR RVSRPVNRLT FASLLLAGGK LDVRVPANGR GELAQLSSSF NAMAEAVQRS
     EERQRRLVAD VAHELRTPLS NLRGYLEGLS DGVVEPSRDL FASLHEETLL QGRILDDLQV
     LALAEAGNLG YTRTPVDLAD LVGNGSTAHR AVAKEAGIAL TVDVPAPVRV EADPDRLRQV
     LGNLLTNAIR YTDAGGHVLV RVREEASEAV LTVEDTGVGM TEADLSRVFD RFWRADPARQ
     RATGGTGLGM TIAHRIVTDH GGRIEVTSEL GKGTKFTVHL PIATATVSAG RRR
//
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