ID R1G189_9PSEU Unreviewed; 1511 AA.
AC R1G189;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=H480_27506 {ECO:0000313|EMBL:EOD65272.1};
OS Amycolatopsis vancoresmycina DSM 44592.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=1292037 {ECO:0000313|EMBL:EOD65272.1, ECO:0000313|Proteomes:UP000014139};
RN [1] {ECO:0000313|EMBL:EOD65272.1, ECO:0000313|Proteomes:UP000014139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44592 {ECO:0000313|EMBL:EOD65272.1,
RC ECO:0000313|Proteomes:UP000014139};
RA Kumar S., Kaur N., Kaur C., Raghava G.P.S., Mayilraj S.;
RT "Draft genome sequence of Amycolatopsis vancoresmycina strain DSM 44592T.";
RL Submitted (FEB-2013) 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 -!- 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:EOD65272.1}.
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; AOUO01000429; EOD65272.1; -; Genomic_DNA.
DR RefSeq; WP_003101551.1; NZ_AOUO01000429.1.
DR PATRIC; fig|1292037.4.peg.5187; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG1511; Bacteria.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG4251; Bacteria.
DR OrthoDB; 9810730at2; -.
DR Proteomes; UP000014139; 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; 8.
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; -; 5.
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; 8.
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; 8.
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; 3.
DR PROSITE; PS50885; HAMP; 8.
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:EOD65272.1};
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 19..65
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 105..157
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 197..249
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 289..341
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 381..433
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 473..525
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 565..617
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 657..709
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 962..1193
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1392..1509
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 883..952
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1442
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1511 AA; 160820 MW; 2D29BFDEAA7F0891 CRC64;
MVEGTRPGTG VGEAGEQELR RLLAGLTAVR DGDFGIRLPG GTDGLLGEIA TVFNGMADQL
SLFTSEVTRV AREVGSEGQL GGQAKVPGVS GTWKDLTDSV NAMAGNLTTQ VRDIAQVATA
VAKGDLSQKI DVDARGEILE LKDTVNTMVD QLSSFADEVT RVAREVGSEG RLGGQAQVPG
VGGVWRDLTD SVNFMAGNLT DQVRNVAQVT TAVAKGDLSQ KITVDARGEI LELKSTINTM
VDQLSSFADE VTRVAREVGT EGRLGGQADV KGVSGTWRDL TDSVNFMAGN LTDQVRNIAQ
VATAVAKGDL SQKINVTARG EVLELKDTLN TMVDQLSAFA DEVTRVAREV GTEGRLGGQA
DVKGVSGTWK DLTESVNVMA DNLTAQVRSI AQVTTAVARG DLSQKIRVDA RGEILELKDT
INTMVDQLSA FADEVTRVAR EVGTEGNLGG QATVRGVSGT WKNLTDNVNV MASNLTGQVR
SIAQVATAVA RGDLSGKITV EAKGEVAALA DVINTMVDTL SAFADEVTRV AREVGTEGML
GGQARVPNVA GTWKDLTDNV NSMANNLTGQ VRNIAQVTTA VAQGDLTRKI DVDARGEILE
LKTTINTMVD QLSAFAAEVT RVAREVGSEG RLGGQAEVEG VSGTWKRLTE NVNELAGNLT
RQVRAIAEVT SAVAEGDLTR SITVDASGEV AELKDNINSM VESLRETTRA NQEQDWLKSN
LATITGLMQG RRDLAVVAAA VMDELVPLVN AQYGAFYLAD DTADVPELRL VGAYGHPDDG
DGPAVRFRVG QSLVGQAARS RRAIAVDDVP PGYATISSGL GSTAPANLIV LPIVVEDQVL
GVIELASVHG FTTVHRAFLE LLMEQIGVNV NSIVANARTD ELLGESQRLT AELQARSEEL
QARQEELQSS NAELEEKAAL LVTQNRDIET KNLEIEQARQ ELEARAQQLT LASKYKSEFL
ANMSHELRTP LNSLLILAQL LAQNPTRNLT AKQVEYAGII HSAGSDLLQL INDILDLSKV
EAGKMDVTPE QVSLRQLIDY VEATFRPMTS QRNLDFRITV APGSPPELLT DDSRLRQVLR
NLLSNAVKFT EVGVIELHIE PVDPERLPRP LRAHGPAVAF RVTDTGIGIA EHQLESIFGA
FQQADGTTSR KYGGTGLGLS ISREIAQLLG GVITAESTLG EGSTFTFSLP VARPDFAPLP
AGEHPGTALA TTDSGAALVS SGPRPYRRLL VVEERQHGLL TLVAESAAAD LADSRDIGLS
PADVEVVTAV GTQEAAAALA TDAYHCVVLD LDLPDRTAFT FLDAMQGDSA LRLVPVLAHN
SRRLDVELEQ LVQSRADVQS LEVLSGLDEL RERIALHLSA EEPGAVLPLV RPDEPAAPVR
AADVDTTLAG RTVLIVDDDP RNVYALTGIL ELHGMQVLHA EDGRKGVETV AAHPGIDLIL
MDVMMPEMDG YTATAKIRAM PEHAGIPIVA VTAKAMPGDR EKSLASGATD YVTKPVDADD
LISRIKRHVT A
//
