ALBA1_SACS2
ID ALBA1_SACS2 Reviewed; 97 AA.
AC P60849; P74761; Q97ZF6;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=DNA/RNA-binding protein Alba 1;
DE AltName: Full=Sso10b;
GN Name=albA1; Synonyms=sso10b; OrderedLocusNames=SSO0962;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RA Wu X.Q., Oppermann M., Knapp S., Berndt K.D., Bergman T., Joernvall H.,
RA Oppermann U.C.T.;
RT "Thermostable DNA-binding proteins from extremophilic Archaea,
RT characterization and heterologous expression of 10kDa proteins from
RT Sulfolobus solfataricus and Sulfolobus shibatae.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [3]
RP ACETYLATION AT SER-2 AND LYS-17, REGULATION OF ACTIVITY, MASS SPECTROMETRY,
RP AND MUTAGENESIS OF LYS-16 AND LYS-17.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11935028; DOI=10.1126/science.1070506;
RA Bell S.D., Botting C.H., Wardleworth B.N., Jackson S.P., White M.F.;
RT "The interaction of Alba, a conserved archaeal chromatin protein, with Sir2
RT and its regulation by acetylation.";
RL Science 296:148-151(2002).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=12198167; DOI=10.1093/emboj/cdf465;
RA Wardleworth B.N., Russell R.J.M., Bell S.D., Taylor G.L., White M.F.;
RT "Structure of Alba: an archaeal chromatin protein modulated by
RT acetylation.";
RL EMBO J. 21:4654-4662(2002).
CC -!- FUNCTION: Binds double-stranded DNA tightly but without sequence
CC specificity. It is distributed uniformly and abundantly on the
CC chromosome, suggesting a role in chromatin architecture. May be
CC involved in DNA compaction. May bind rRNA and mRNA, playing a role in
CC maintaining the structural and functional stability of RNA, and,
CC perhaps, ribosomes.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- INTERACTION:
CC P60849; P60849: albA1; NbExp=2; IntAct=EBI-9021190, EBI-9021190;
CC P60849; Q97ZF4: albA2; NbExp=6; IntAct=EBI-9021190, EBI-9021196;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Chromosome
CC {ECO:0000305}.
CC -!- PTM: Acetylated. Deacetylation by the SIR2-homolog deacetylase
CC increases its DNA-binding affinity, thereby repressing transcription.
CC Regulation of DNA-based activities is therefore achieved at the
CC chromatin level. {ECO:0000269|PubMed:11935028}.
CC -!- MASS SPECTROMETRY: Mass=10538; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:11935028};
CC -!- SIMILARITY: Belongs to the histone-like Alba family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK41236.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ298830; CAC12668.1; -; Genomic_DNA.
DR EMBL; AE006641; AAK41236.1; ALT_INIT; Genomic_DNA.
DR PIR; E90247; E90247.
DR RefSeq; WP_009992406.1; NC_002754.1.
DR PDB; 1H0X; X-ray; 2.60 A; A/B=1-97.
DR PDB; 1H0Y; X-ray; 2.80 A; A=1-97.
DR PDB; 2BKY; X-ray; 1.70 A; A/B=1-97.
DR PDB; 4R3L; X-ray; 1.84 A; B=2-7.
DR PDBsum; 1H0X; -.
DR PDBsum; 1H0Y; -.
DR PDBsum; 2BKY; -.
DR PDBsum; 4R3L; -.
DR AlphaFoldDB; P60849; -.
DR BMRB; P60849; -.
DR SMR; P60849; -.
DR DIP; DIP-48444N; -.
DR IntAct; P60849; 1.
DR STRING; 273057.SSO0962; -.
DR iPTMnet; P60849; -.
DR EnsemblBacteria; AAK41236; AAK41236; SSO0962.
DR GeneID; 7812521; -.
DR GeneID; 7940586; -.
DR GeneID; 8761191; -.
DR KEGG; sso:SSO0962; -.
DR PATRIC; fig|273057.12.peg.960; -.
DR eggNOG; arCOG01753; Archaea.
DR HOGENOM; CLU_110989_1_0_2; -.
DR InParanoid; P60849; -.
DR OMA; QFNEGAK; -.
DR PhylomeDB; P60849; -.
DR EvolutionaryTrace; P60849; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0030261; P:chromosome condensation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.110.20; -; 1.
DR HAMAP; MF_01122; AlbA; 1.
DR InterPro; IPR036882; Alba-like_dom_sf.
DR InterPro; IPR013795; DNA/RNA-bd_Alba.
DR InterPro; IPR002775; DNA/RNA-bd_Alba-like.
DR Pfam; PF01918; Alba; 1.
DR PIRSF; PIRSF028732; Alba; 1.
DR SUPFAM; SSF82704; SSF82704; 1.
DR TIGRFAMs; TIGR00285; TIGR00285; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chromosome; Cytoplasm; DNA condensation;
KW DNA-binding; Reference proteome; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11935028"
FT CHAIN 2..97
FT /note="DNA/RNA-binding protein Alba 1"
FT /id="PRO_0000151712"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:11935028"
FT MOD_RES 17
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:11935028"
FT MUTAGEN 16
FT /note="K->A,V: Unable to repress transcription."
FT /evidence="ECO:0000269|PubMed:11935028"
FT MUTAGEN 17
FT /note="K->A,V: Unable to repress transcription."
FT /evidence="ECO:0000269|PubMed:11935028"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:2BKY"
FT HELIX 19..31
FT /evidence="ECO:0007829|PDB:2BKY"
FT STRAND 36..42
FT /evidence="ECO:0007829|PDB:2BKY"
FT HELIX 45..59
FT /evidence="ECO:0007829|PDB:2BKY"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:2BKY"
FT STRAND 65..79
FT /evidence="ECO:0007829|PDB:2BKY"
FT STRAND 84..96
FT /evidence="ECO:0007829|PDB:2BKY"
SQ SEQUENCE 97 AA; 10585 MW; 22C1BC9CCDB6B013 CRC64;
MSSGTPTPSN VVLIGKKPVM NYVLAALTLL NQGVSEIVIK ARGRAISKAV DTVEIVRNRF
LPDKIEIKEI RVGSQVVTSQ DGRQSRVSTI EIAIRKK
