ID W2ESK3_9ACTN Unreviewed; 1404 AA.
AC W2ESK3;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=MPTA5024_18210 {ECO:0000313|EMBL:ETK34703.1};
OS Microbispora sp. ATCC PTA-5024.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Microbispora.
OX NCBI_TaxID=316330 {ECO:0000313|EMBL:ETK34703.1, ECO:0000313|Proteomes:UP000018869};
RN [1] {ECO:0000313|EMBL:ETK34703.1, ECO:0000313|Proteomes:UP000018869}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC PTA-5024 {ECO:0000313|EMBL:ETK34703.1,
RC ECO:0000313|Proteomes:UP000018869};
RX PubMed=24459268;
RA Sosio M., Gallo G., Pozzi R., Serina S., Monciardini P., Bera A.,
RA Stegmann E., Weber T.;
RT "Draft Genome Sequence of the Microbispora sp. Strain ATCC-PTA-5024,
RT Producing the Lantibiotic NAI-107.";
RL Genome Announc. 2:e01198-13(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:ETK34703.1}.
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DR EMBL; AWEV01000135; ETK34703.1; -; Genomic_DNA.
DR RefSeq; WP_051458286.1; NZ_KI866523.1.
DR STRING; 316330.MPTA5024_18210; -.
DR PATRIC; fig|316330.3.peg.3527; -.
DR HOGENOM; CLU_000445_3_1_11; -.
DR OrthoDB; 9810730at2; -.
DR Proteomes; UP000018869; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
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; 7.
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; 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; 6.
DR Pfam; PF18947; HAMP_2; 1.
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; 7.
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; 3.
DR PROSITE; PS50885; HAMP; 7.
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:ETK34703.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000018869};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 106..160
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 200..252
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 292..344
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 384..436
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 476..528
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 568..620
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 660..712
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 960..1193
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1261..1378
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1382..1404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 874..929
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1311
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1404 AA; 152467 MW; CAAB7FE9C75F45D7 CRC64;
MSPANVELAG TERVYTESDL VPFLETLITW RDGDFRRRVS HAPPGILSEI RLLLNEVADR
REHLANELGR VRREIVKEGR FDERLSPGPG VGAWAESVGS VNDLIDALVS PVTGAADVID
AVAKGDLSRR IDLDRGARGE VRRLGKAVNG MVEQLSAFAA EVTRVAREVG TEGRLGGRAN
LRGMSGSWRD LTEAVNTMSG RVSAQVRDIA EVTTAVARGD LSRKVTVDAV GEMLELKNTV
NTMVDQLSAF AEEVTRVARE VGTEGKLGGQ AQVRGVSGVW KDLTDNVNFM ANNLTSQVRQ
IAAVSTAVAQ GNLSKKITVD AQGEILELKD TLNTMVDQLS AFAAEVTRVA REVGTEGRLG
GRAEVKGVSG VWKDLTDNVN SMTNNLTYQV RNIAQVTTAV ANGDLTRKID VDAQGEILEL
KSTMNTMVDQ LSSFASEVTR VAREVGTEGR LGGQAQVRGV SGIWKDLTDN VNFMANNLTS
QVRQIAAVST AVAQGNLSRK ITVDAQGEIL ELKDTMNTMV DQLSAFADEV TRVAREVGTE
GRLGGQARVQ GVSGVWKDLT DNVNSMANNL TYQVRNIAQV TTAVANGDLT RKIDVDAQGE
ILELKSTMNK MVDQLSSFAS EVTRVAREVG SEGQLGGQAR VEGVEGTWKR LTESVNELAG
NLTTQVRAIA EVTSAVARGD LTRSITVAAP GELAQLKDTI NTMVATLRET TKANEEQDWL
KSNLARISRL MQGHRDLMEV SRLIMSELTP LVTASHGACY LVTDDRLELI AGYGIQPGSS
PRQSFAMGEG IIGQAALEAK QTILQNVPPE SIVIETGLSR SRPAQIVVLP ILFENKVLGV
LEMATFTEFG EAHLAFLTQL VETIGVTINT IMANSRTEDL LKESQRLALE LQERSDELQR
QQEELRRSNA ELEDKAALLA KQNRAIEIQN FQIEQARRTL EERAEQLAVS SRYKSEFLAN
MSHELRTPLN SLLVLAKLLT ENAEGNLTPQ QVEFARTIHD AGSALLQLIN DILDLTKVEA
GRMDIHPQQL SLPTLVDYME ATFAPLAQDK GLSFTVEVDP SVPNSLSTDE QRLQQVLRNL
LSNAVKFTPK GEVRLEVTHA PADIAYVDDT LKGASDILAF KVIDTGIGIA PDKLEIIFEQ
FRQADGTTSR KYGGTGLGLS ICREIARLLG GEIHVDSAPG LGSTFTLFLP LAYVGPLASP
DGGATTPGGQ TDNRPVEVPE LHTRDVLPEI PLPTDLPSPQ AVAPIVDGRD WQGDDPLTGA
KILIVDDDIR NVFALTSVLE RHGSTVVYAE NGREGIEQLE RNEDVALVLM DIMMPEMDGW
ATTSAIRMMP QFADLPIIAL TAKVMRGDRE KSIASGASDY VPKPVDVDRL LERLRGWLLR
GRGNGADRPR PAPPVDHRDI HEEA
//
