ID Q63R44_BURPS Unreviewed; 135 AA.
AC Q63R44;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE SubName: Full=Heat shock protein 15 {ECO:0000313|EMBL:CAH36840.1};
GN Name=hslR {ECO:0000313|EMBL:CAH36840.1};
GN OrderedLocusNames=BPSL2830 {ECO:0000313|EMBL:CAH36840.1};
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560 {ECO:0000313|EMBL:CAH36840.1, ECO:0000313|Proteomes:UP000000605};
RN [1] {ECO:0000313|EMBL:CAH36840.1, ECO:0000313|Proteomes:UP000000605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243 {ECO:0000313|EMBL:CAH36840.1,
RC ECO:0000313|Proteomes:UP000000605};
RX PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.M., Atkins T.,
RA Crossman L.C., Pitt T., Churcher C., Mungall K., Bentley S.D., Sebaihia M.,
RA Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A., Brown N.F.,
RA Challis G.L., Cherevach I., Chillingworth T., Cronin A., Crosset B.,
RA Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z., Hauser H.,
RA Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S., Price C.,
RA Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M.,
RA Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., Whitehead S.,
RA Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT pseudomallei.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
CC -!- SIMILARITY: Belongs to the HSP15 family.
CC {ECO:0000256|ARBA:ARBA00008396}.
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DR EMBL; BX571965; CAH36840.1; -; Genomic_DNA.
DR RefSeq; WP_004194347.1; NZ_CP009538.1.
DR RefSeq; YP_109424.1; NC_006350.1.
DR AlphaFoldDB; Q63R44; -.
DR STRING; 272560.BPSL2830; -.
DR GeneID; 56594681; -.
DR KEGG; bps:BPSL2830; -.
DR PATRIC; fig|272560.51.peg.2472; -.
DR eggNOG; COG1188; Bacteria.
DR Proteomes; UP000000605; Chromosome 1.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0043023; F:ribosomal large subunit binding; IEA:InterPro.
DR GO; GO:0003727; F:single-stranded RNA binding; IEA:InterPro.
DR GO; GO:0034605; P:cellular response to heat; IEA:InterPro.
DR CDD; cd00165; S4; 1.
DR Gene3D; 3.10.290.10; RNA-binding S4 domain; 1.
DR InterPro; IPR025708; HSP15.
DR InterPro; IPR002942; S4_RNA-bd.
DR InterPro; IPR036986; S4_RNA-bd_sf.
DR Pfam; PF01479; S4; 1.
DR PIRSF; PIRSF016821; HSP15; 1.
DR SMART; SM00363; S4; 1.
DR SUPFAM; SSF55174; Alpha-L RNA-binding motif; 1.
DR PROSITE; PS50889; S4; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Reference proteome {ECO:0000313|Proteomes:UP000000605};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00182}; Stress response {ECO:0000313|EMBL:CAH36840.1}.
FT DOMAIN 13..74
FT /note="RNA-binding S4"
FT /evidence="ECO:0000259|SMART:SM00363"
FT REGION 111..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 135 AA; 15296 MW; 41C0E7FF03765990 CRC64;
MNFKISTEPG ARLRIDKWLW AARFFKTRSL AADAVEKGRV RIGGAAVKPA KEVRVGDRVD
VTIERVVWEI DVLGVCDVRG PASVAQTLYA ETEAGRAKRL AELERRRHFR EPSAELHGRP
TKRDRRIIDR FSNGS
//
