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SSB_PROMI
ID   SSB_PROMI               Reviewed;         174 AA.
AC   P28046;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=Single-stranded DNA-binding protein {ECO:0000255|HAMAP-Rule:MF_00984};
DE            Short=SSB {ECO:0000255|HAMAP-Rule:MF_00984};
GN   Name=ssb;
OS   Proteus mirabilis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=584;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PG1300;
RX   PubMed=8012606; DOI=10.1099/00221287-140-4-889;
RA   de Vries J., Wackernagel W.;
RT   "Cloning and sequencing of the Proteus mirabilis gene for a single-stranded
RT   DNA-binding protein (SSB) and complementation of Escherichia coli ssb point
RT   and deletion mutations.";
RL   Microbiology 140:889-895(1994).
RN   [2]
RP   FUNCTION, DNA-BINDING, AND SUBUNIT.
RX   PubMed=7925378; DOI=10.1111/j.1432-1033.1994.00613.x;
RA   de Vries J., Genschel J., Urbanke C., Thole H., Wackernagel W.;
RT   "The single-stranded-DNA-binding proteins (SSB) of Proteus mirabilis and
RT   Serratia marcescens.";
RL   Eur. J. Biochem. 224:613-622(1994).
CC   -!- FUNCTION: Plays an important role in DNA replication, recombination and
CC       repair. Binds to ssDNA and to an array of partner proteins to recruit
CC       them to their sites of action during DNA metabolism (Probable).
CC       {ECO:0000305|PubMed:7925378}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00984,
CC       ECO:0000269|PubMed:7925378}.
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DR   EMBL; X65079; CAA46206.1; -; Genomic_DNA.
DR   PIR; S19955; S19955.
DR   RefSeq; WP_004249162.1; NZ_WURR01000005.1.
DR   AlphaFoldDB; P28046; -.
DR   SMR; P28046; -.
DR   STRING; 584.AOUC001_01755; -.
DR   PRIDE; P28046; -.
DR   GeneID; 6802769; -.
DR   OMA; GQMQERT; -.
DR   OrthoDB; 1942216at2; -.
DR   GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR   CDD; cd04496; SSB_OBF; 1.
DR   Gene3D; 2.40.50.140; -; 1.
DR   HAMAP; MF_00984; SSB; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR000424; Primosome_PriB/ssb.
DR   InterPro; IPR011344; ssDNA-bd.
DR   PANTHER; PTHR10302; PTHR10302; 1.
DR   Pfam; PF00436; SSB; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00621; ssb; 1.
DR   PROSITE; PS50935; SSB; 1.
PE   1: Evidence at protein level;
KW   DNA damage; DNA recombination; DNA repair; DNA replication; DNA-binding.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..174
FT                   /note="Single-stranded DNA-binding protein"
FT                   /id="PRO_0000096076"
FT   DOMAIN          6..111
FT                   /note="SSB"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT   DNA_BIND        55..61
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT   REGION          110..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           169..174
FT                   /note="Important for interaction with partner proteins"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT   COMPBIAS        118..148
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   174 AA;  18831 MW;  6A13B9A813CD2583 CRC64;
     MASRGVNKVI LIGNLGQDPE IRYMPSGGAV ANLTLATSES WRDKQTGEMK EKTEWHRVVI
     FGKLAEIAGE YLRKGSQVYI EGQLQTRKWQ DQSGQDRYST EVVVNIGGTM QMLGGRGGQD
     NAPSQGQGGW GQPQQPQASQ QFSGGAPSRP AQQPAAAPAP SNEPPMDFDD DIPF
 
 
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