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Database: UniProt
Entry: F2R5Z8_STRVP
LinkDB: F2R5Z8_STRVP
Original site: F2R5Z8_STRVP 
ID   F2R5Z8_STRVP            Unreviewed;      1337 AA.
AC   F2R5Z8;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=SVEN_0372 {ECO:0000313|EMBL:CCA53659.1};
OS   Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM
OS   4526 / NBRC 13096 / PD 04745).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=953739 {ECO:0000313|EMBL:CCA53659.1, ECO:0000313|Proteomes:UP000006854};
RN   [1] {ECO:0000313|EMBL:CCA53659.1, ECO:0000313|Proteomes:UP000006854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 /
RC   PD 04745 {ECO:0000313|Proteomes:UP000006854};
RX   PubMed=21463507; DOI=10.1186/1471-2164-12-175;
RA   Pullan S.T., Bibb M.J., Merrick M.;
RT   "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae
RT   provides new insights into global nitrogen regulation in actinomycetes.";
RL   BMC Genomics 12:175-175(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; FR845719; CCA53659.1; -; Genomic_DNA.
DR   STRING; 953739.SVEN_0372; -.
DR   KEGG; sve:SVEN_0372; -.
DR   PATRIC; fig|953739.5.peg.5940; -.
DR   eggNOG; COG0745; Bacteria.
DR   eggNOG; COG1511; Bacteria.
DR   eggNOG; COG2203; Bacteria.
DR   eggNOG; COG4251; Bacteria.
DR   HOGENOM; CLU_000445_3_0_11; -.
DR   Proteomes; UP000006854; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd06225; HAMP; 6.
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; 1.20.120.1530; -; 4.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
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:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   Pfam; PF13185; GAF_2; 1.
DR   Pfam; PF00672; HAMP; 5.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00304; HAMP; 6.
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; 2.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 2.
DR   PROSITE; PS50885; HAMP; 6.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CCA53659.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000006854};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          25..71
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          111..163
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          203..255
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          295..347
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          387..439
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          479..531
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          783..1014
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1217..1334
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          711..773
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         1267
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1337 AA;  142423 MW;  36629B48273A28EB CRC64;
     MSDMTTEGSS VRVRPGPAAV GEPELRQLLA GLTAVRDGDF GTRLPDEADG LMGEISLVFN
     GMVDQLSLFT SEVTRVAREV GTEGTLGGQA AVPGVSGTWA DLTDSVNAMA GNLTTQVRDI
     AQVATAVARG DLSQKIDVDA HGEILELKNT INTMVDQLSS FADEVTRMAR DVGTEGILGG
     QADVKGASGT WRDLTDSVNS MAGNLTAQVR AIAHVATAVA NGDLSKKVDV DARGEILELK
     TTINTMVDQL SAFADEVTRV AREVGTEGNL GGQATVRGAS GTWKDLTDNV NVMASNLTGQ
     VRSIAQVATS VARGDLSRRI TVEAKGEVAA LADTINTMVD TLSAFADEVT RVAREVGTEG
     RLGGQARVPN VAGTWKDLTD NVNSMANNLT GQVRNIAQVT TAVANGDLSK KIDVDARGEI
     LELKTTINTM VDQLSSFAAE VTRVAREVGS EGRLGGQAEV EGVSGTWKRL TENVNELAGN
     LTRQVRAIAE VASAVAEGDL TRSITVEASG EVAELKDNIN AMVGSLRETT RANQEQDWLK
     SSLARISALM QGHRDLAVVA ELVMDELTPL VAAQYGAFYL AEEGTDGVEL GLVGSYGRPA
     GDQGRDRFRL GESLVGQAAR SRRTIAAENV PADYVTISSG LGSTSRGSLV VLPVVVEDQV
     LGVIELMSFT PFTSVHRDFL EQLMETVGVN LSTIVANART DELLDESQRL AGELRSRTEE
     LQVRQEELQR SNAELEEKAA LLATQNRDIE AKNLQIEQAR QELEDRAQQL ALASTYKSEF
     LANMSHELRT PLNSLLILAQ LLAQNPTRNL TAKQVEYAGI IHSAGSDLLQ LINDILDLSK
     VEAGKMDFNP ERVPLRRLLD YVEATFRPLT TQKSLAFSVT TAAGVPVDLV TDDSRLRQVL
     RNLLSNAVKF TEHGSVELRI EPASDAELPV PVHRGGPVVA FRVTDTGIGI APENLEAIFG
     AFQQADGTTN RKYGGTGLGL SISREIAFLL GGALTVTSVA GEGSTFTLYL PVTRTDVTEK
     PAARQLEAAE VSVPALEAAP APAAGPGTAT ARPTRRLLVI EERPRGLLAV VAENAVTQLS
     ADGGHAERTD IELIAVVGPQ EAAAALADQP FHCVVLDLDM ADGDALRFLA AMDGDEALRT
     VPVLAHNNRR LPADEEGALQ ELARRRPLEL LSSLDELRER IALHLSAEQP GDVVPLVRGD
     HWAPAPQAID TTLHGRTVLV VDDDARNLYA LSGILELHGV TVLHAENGRK GIETLLANPA
     VSLVLMDVMM PEMDGYTATA RIRELSQYAD LPVIAVTAKA MPGDREKSLA SGASDYVTKP
     VDADELIACI GRWLNDG
//
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