ID V6KE95_STRNV Unreviewed; 1846 AA.
AC V6KE95;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=M877_09885 {ECO:0000313|EMBL:EST30417.1};
OS Streptomyces niveus NCIMB 11891.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1352941 {ECO:0000313|EMBL:EST30417.1, ECO:0000313|Proteomes:UP000017971};
RN [1] {ECO:0000313|EMBL:EST30417.1, ECO:0000313|Proteomes:UP000017971}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 11891 {ECO:0000313|EMBL:EST30417.1,
RC ECO:0000313|Proteomes:UP000017971};
RX PubMed=24407644;
RA Flinspach K., Ruckert C., Kalinowski J., Heide L., Apel A.K.;
RT "Draft Genome Sequence of Streptomyces niveus NCIMB 11891, Producer of the
RT Aminocoumarin Antibiotic Novobiocin.";
RL Genome Announc. 2:e01146-e01113(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};
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:EST30417.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AWQW01000068; EST30417.1; -; Genomic_DNA.
DR STRING; 193462.BBN63_08130; -.
DR PATRIC; fig|1352941.4.peg.2026; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG0840; Bacteria.
DR eggNOG; COG1511; Bacteria.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG2770; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_3_0_11; -.
DR Proteomes; UP000017971; 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; 11.
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; -; 7.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 1.10.8.500; HAMP domain in histidine kinase; 1.
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; 8.
DR Pfam; PF18947; HAMP_2; 2.
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; 12.
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; 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; 6.
DR PROSITE; PS50885; HAMP; 12.
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:EST30417.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 25..74
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 114..179
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 219..271
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 311..363
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 403..455
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 495..547
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 587..639
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 679..731
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 771..823
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 863..915
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 955..1007
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1047..1099
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1361..1602
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1726..1843
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1634..1715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1282..1351
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1776
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1846 AA; 197129 MW; BC7305E9EA9E1BC7 CRC64;
MAARGNSTRA KGGRSRNNGA IEVDAAALNR LLTALVAMRD GNFRKRLTVS GDDVMAEISA
VFNEVADRNL HLTGELARVR RMVGREGKLT ERLETGACEG SWATAIDASN ALVDDLARPV
SEVGRVLSAV AEGDLEQRME LRSHFDEGSA GTERPLRGEF LKVARTVNSL VDQLSAFTDE
VTRVALEVGT EGKLGGQAKV RGMSGSWKDL TDSVNTMAYR LTAQVRDIAL VTTAVAKGDL
SRKVTVHVAG EMLQLKNTVN TMVDQLSSFS SEVTRVAREV GTEGELGGQA TVPGVAGVWK
DLTDSVNTMA GNLTSQVRGI AEVTTAVANG DLSQKVTVSA RGEVAQLAET INQMTETLRT
FADEVTRVAS EVGGSGVLGG QAQVPGAAGT WKDLTDSVNT VFRNLTTQVR DIAQVTTAVA
NGDLSQKVTV DVAGEMLELK NTVNTMVRQL NSFGSEVTRV AREVGVEGQL GGQAEVPGAA
GTWKDLTDSV NTAFHNLTGQ VRDIAQVTTA VANGDLSQKV TVNVAGEMLE LKNTVNTMVA
QLSSFADQVT RMARDVGTEG RLGGQARVDG VSGTWKELTD SVNFMAGNLT DQVRQIAQVT
TAVARGDLSQ KIDVDARGEI LELKNTINTM VDQLSAFAEQ VTRVAREVGT DGRLGGQAQV
PGVAGVWRDL TDSVNGMAGN LTSQVRNIAQ VATAVARGDL SQKIDVDARG EILELKNTLN
TMVDQLSNFA EQVTRVAREV GTEGMLGGQA EVQGVSGTWK DLTQSVNFMA NNLTSQVRNI
AEVTTAVAKG DLSKKITVDA KGEILDLVTT VNTMVDQLSN FADEVTRVAR EVGTEGILGG
QARVRGVTGI WKDLSDNVNT MANNLTSQVR NISRVSSAVA NGDLTKKVTV EARGEVAELA
DTVNIMVTTL SSFADEVTRV AREVGTEGEL GGQARVPGVS GTWKDLTESV NSMASNLTGQ
VRQIATVTTA IAKGDLTKKI DIDARGEIQE LKNTINTMVD QLSSFADQVT RVAREVGTDG
QLGGQARVRD VDGTWRDLTE SVNEMAGNLT RQVRAIAAVA TAVTRGDLNL KIDVDAAGEI
QVLQDNINTM IANLRDTTLA NEEQDWLKGN LARISGLMQG RRDLDDVASL IMSELTPVVA
AQHGAFFLAM PTGTVSELGT GGGRDGSYEL CMRGSYGYSA GSMPTSFRPG ETLIGTAAEE
KRTIQVNVPP GYLKISSGLG EASPAYVIVL PVLFEGKVLG VIELASFQPF TQIQRDFLNQ
IAEMIATSVN TISVNTKTEV LLKQSQELTE QLRERSAELE NRQKALQSSN AELEEKAELL
ARQNRDIEVK NTEIEEARQV LEERAEQLAV SMRYKSEFLA NMSHELRTPL NSLLILAKLL
ADNAEMNLSP KQVEFAETIH GAGSDLLQLI NDILDLSKVE AGKMDVSPTR IALVQLVDYV
EATFRPLTAE KGLDFSVRVS PELPATLHTD EQRLLQVLRN LLSNAVKFTD TGAVELVIRP
AGADVPNAIR EQLLEAGSLR DADADLIAFS VTDTGIGIAA SKMRVIFEAF KQADGTTSRK
YGGTGLGLSI SREIARLLGG EIHAASEPGR GSTFTLYLPL HASELPPQGY PQLAPGIDPQ
RGGSDYSALS AERARLDRPA APSEARTGPA ALFRRRRKAL GGPEQLNSLS GRPGGASGDL
PGGGNGSAGA ANGARPSGVS GAQEPWAPDA QDAPEERRTF SFGGEKVLIV DDDIRNVFAL
TSVLEQHGLS VLYAENGREG IEVLEQHDDV TLVLMDIMMP EMDGYATTTA IRRMPQFAGL
PIIALTAKAM KGDREKAIDS GASDYVTKPV DPDHLLSVME QWMHQK
//
