ALBA1_SACSH
ID ALBA1_SACSH Reviewed; 97 AA.
AC P60848; P74761; Q97ZF6;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=DNA/RNA-binding protein Alba 1;
DE AltName: Full=Ssh10b;
GN Name=albA1; Synonyms=ssh10b;
OS Saccharolobus shibatae (Sulfolobus shibatae).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=2286;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12;
RX PubMed=8972852; DOI=10.1093/nar/24.23.4668;
RA Jaxel C., Bouthier de la Tour C., Duguet M., Nadal M.;
RT "Reverse gyrase gene from Sulfolobus shibatae B12: gene structure,
RT transcription unit and comparative sequence analysis of the two domains.";
RL Nucleic Acids Res. 24:4668-4675(1996).
RN [2]
RP CHARACTERIZATION.
RC STRAIN=ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12;
RX PubMed=10869069; DOI=10.1128/jb.182.14.3929-3933.2000;
RA Xue H., Guo R., Wen Y., Liu D., Huang L.;
RT "An abundant DNA binding protein from the hyperthermophilic archaeon
RT Sulfolobus shibatae affects DNA supercoiling in a temperature-dependent
RT fashion.";
RL J. Bacteriol. 182:3929-3933(2000).
RN [3]
RP CHARACTERIZATION OF DIMER CONFORMATIONS, AND MUTAGENESIS OF PRO-8 AND
RP PRO-62.
RX PubMed=14523014; DOI=10.1074/jbc.m308510200;
RA Cui Q., Tong Y., Xue H., Huang L., Feng Y., Wang J.;
RT "Two conformations of archaeal Ssh10b. The origin of its temperature-
RT dependent interaction with DNA.";
RL J. Biol. Chem. 278:51015-51022(2003).
RN [4]
RP BINDING TO RNA, AND SUBCELLULAR LOCATION.
RX PubMed=14651642; DOI=10.1046/j.1365-2958.2003.03793.x;
RA Guo R., Xue H., Huang L.;
RT "Ssh10b, a conserved thermophilic archaeal protein, binds RNA in vivo.";
RL Mol. Microbiol. 50:1605-1615(2003).
RN [5]
RP REVIEW.
RX PubMed=14519199; DOI=10.1186/gb-2003-4-10-r64;
RA Aravind L., Iyer L.M., Anantharaman V.;
RT "The two faces of Alba: the evolutionary connection between proteins
RT participating in chromatin structure and RNA metabolism.";
RL Genome Biol. 4:R64.1-R64.10(2003).
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. Binds rRNA and mRNA in vivo. May play a
CC role in maintaining the structural and functional stability of RNA,
CC and, perhaps, ribosomes.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Highly active above 45 degrees Celsius. Poorly active at 25 degrees
CC Celsius.;
CC -!- SUBUNIT: Homodimer. Two forms exist in solution due to isomerization of
CC the Leu-61/Pro-62 peptide bond. The trans (T) form of the dimer
CC dominates at higher temperatures, whereas the population of the cis (C)
CC form increases at lower temperatures. The T form causes DNA to adopt a
CC supercoiled conformation.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14651642}.
CC Chromosome {ECO:0000269|PubMed:14651642}.
CC -!- PTM: Acetylated. Deacetylation by the SIR2-homolog deacetylase may
CC regulate its activity (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the histone-like Alba family. {ECO:0000305}.
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DR EMBL; X98420; CAA67066.1; -; Genomic_DNA.
DR PIR; T29101; T29101.
DR RefSeq; WP_009992406.1; NZ_CP077715.1.
DR PDB; 1Y9X; NMR; -; A/B=1-97.
DR PDB; 3WBM; X-ray; 2.00 A; A/B/C/D=1-97.
DR PDBsum; 1Y9X; -.
DR PDBsum; 3WBM; -.
DR AlphaFoldDB; P60848; -.
DR BMRB; P60848; -.
DR SMR; P60848; -.
DR GeneID; 8761191; -.
DR EvolutionaryTrace; P60848; -.
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:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
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; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..97
FT /note="DNA/RNA-binding protein Alba 1"
FT /id="PRO_0000151711"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250"
FT MOD_RES 17
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MUTAGEN 8
FT /note="P->A: No effect on cis-trans isomerization of
FT dimer."
FT /evidence="ECO:0000269|PubMed:14523014"
FT MUTAGEN 62
FT /note="P->A: Loss of cis-trans isomerization of dimer."
FT /evidence="ECO:0000269|PubMed:14523014"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:3WBM"
FT HELIX 19..31
FT /evidence="ECO:0007829|PDB:3WBM"
FT STRAND 36..42
FT /evidence="ECO:0007829|PDB:3WBM"
FT HELIX 45..59
FT /evidence="ECO:0007829|PDB:3WBM"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:3WBM"
FT STRAND 65..76
FT /evidence="ECO:0007829|PDB:3WBM"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:1Y9X"
FT STRAND 86..96
FT /evidence="ECO:0007829|PDB:3WBM"
SQ SEQUENCE 97 AA; 10585 MW; 22C1BC9CCDB6B013 CRC64;
MSSGTPTPSN VVLIGKKPVM NYVLAALTLL NQGVSEIVIK ARGRAISKAV DTVEIVRNRF
LPDKIEIKEI RVGSQVVTSQ DGRQSRVSTI EIAIRKK
