ID A0A124HCR1_9ACTN Unreviewed; 889 AA.
AC A0A124HCR1;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Histidine kinase {ECO:0000313|EMBL:KUM95197.1};
GN ORFNames=AQI88_17990 {ECO:0000313|EMBL:KUM95197.1};
OS Streptomyces cellostaticus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=67285 {ECO:0000313|EMBL:KUM95197.1, ECO:0000313|Proteomes:UP000054241};
RN [1] {ECO:0000313|EMBL:KUM95197.1, ECO:0000313|Proteomes:UP000054241}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40189 {ECO:0000313|EMBL:KUM95197.1,
RC ECO:0000313|Proteomes:UP000054241};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces cellostaticus DSM 40189, type strain
RT for the species Streptomyces cellostaticus.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:KUM95197.1}.
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; LMWL01000032; KUM95197.1; -; Genomic_DNA.
DR RefSeq; WP_066999823.1; NZ_KQ948022.1.
DR AlphaFoldDB; A0A124HCR1; -.
DR STRING; 67285.AQI88_17990; -.
DR OrthoDB; 118142at2; -.
DR Proteomes; UP000054241; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR CDD; cd16936; HATPase_RsbW-like; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR036457; PPM-type-like_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR InterPro; IPR033463; sCache_3.
DR InterPro; IPR029151; Sensor-like_sf.
DR PANTHER; PTHR43156:SF2; MULTIDOMAIN REGULATORY PROTEIN RV1364C; 1.
DR PANTHER; PTHR43156; STAGE II SPORULATION PROTEIN E-RELATED; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF13581; HATPase_c_2; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF17203; sCache_3_2; 1.
DR Pfam; PF07228; SpoIIE; 1.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00091; PAS; 1.
DR SMART; SM00331; PP2C_SIG; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR SUPFAM; SSF103190; Sensory domain-like; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:KUM95197.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054241};
KW Transferase {ECO:0000313|EMBL:KUM95197.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 219..259
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT REGION 68..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 889 AA; 95467 MW; 95B2AA2F49695B3B CRC64;
MDRQRGRLRS WHGPRTVAGQ VFILQVFIIL VLVAAAVAAL LLQSRTDAER EARNRTLAVA
TAVASSPSVQ QALADPNPTA ALQPQAEETR KRSNVDFVVV MSPEGIRYTH PNPARIGQHY
IGDIAAAQHG GIVTETTTGT LGRSVRTVVP VTTPQGKVIG LVSAGIRVNQ VTVAADRQVP
LVLAATGVVL SAATAGSALI SRRLRRQTHG LGPTQMTRMY EHHDAVLHAV REGVLIIDAQ
GRLLLANDEA RRLLGLEADG EGRPVSGLGL EPRAEQLLLS GTPATDQVIQ VGDRLLAISQ
RPMAQQPGPG GSVATLRDTT ELSVLMGRVE VAQERLKLLY DAGIRIGTTL NVRRTAEELA
ELAVPRFADY VTVDLADAVL RGEEPNLVNM TELRRVALHG IRGDSPLYPP GQLIPFDPST
PQASGFGSGR MVLEADMAAF SGWQAQAPDR ARRLVAYGIH SMIAAPLRAR GVILGVATFW
RSKEPTPFAQ EDLSVAEELV ARAAVSIDNA RRFTREHAMA VTLQRSLLPH ALPEQSAVEV
AHRYLPAEAG LGGVGGDWFD VIPLPGARVA IVVGDVVGHG LHAAATMGQL RTAVHNFSTL
DLPPDELLWY LDELVTRIDQ DRDRDNSETP TLTGATCLYA IYDPVSGLCT MARAGHLEPL
VVDPHGHAEL AGVPAGPPLG LGGLPYEKAE VRLPEGSSIV LYTDGLIEDR QRDIDEGIEQ
LRCAIAHAGR SPDQMCGAVM DALLPTAPRD DVALVIARTR LLDGDRTAVW NVPTEPSAVA
GVRACAGRLL NDWGLDEEAF TLELILSELV TNAIRYATGP ISVRLIRDRS LICEVSDGSS
VSPHLRRATT MDEGGRGLFL VAQFADRWGT RYTADGKVIW TEQQLPTQA
//
