ID   SSB2_LISMO              Reviewed;         160 AA.
AC   Q8Y4X1;
DT   24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Single-stranded DNA-binding protein 2 {ECO:0000255|HAMAP-Rule:MF_00984};
DE            Short=SSB 2 {ECO:0000255|HAMAP-Rule:MF_00984};
GN   Name=ssb2; OrderedLocusNames=lmo2308;
OS   Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=169963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-679 / EGD-e;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
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.
CC       {ECO:0000255|HAMAP-Rule:MF_00984}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00984}.
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; AL591982; CAD00386.1; -; Genomic_DNA.
DR   PIR; AD1363; AD1363.
DR   RefSeq; NP_465832.1; NC_003210.1.
DR   RefSeq; WP_003722552.1; NZ_CP023861.1.
DR   AlphaFoldDB; Q8Y4X1; -.
DR   SMR; Q8Y4X1; -.
DR   STRING; 169963.lmo2308; -.
DR   PaxDb; Q8Y4X1; -.
DR   EnsemblBacteria; CAD00386; CAD00386; CAD00386.
DR   GeneID; 984487; -.
DR   KEGG; lmo:lmo2308; -.
DR   PATRIC; fig|169963.11.peg.2363; -.
DR   eggNOG; COG0629; Bacteria.
DR   HOGENOM; CLU_078758_6_2_9; -.
DR   OMA; INIVIWR; -.
DR   PhylomeDB; Q8Y4X1; -.
DR   BioCyc; LMON169963:LMO2308-MON; -.
DR   Proteomes; UP000000817; Chromosome.
DR   GO; GO:0009295; C:nucleoid; IBA:GO_Central.
DR   GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
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   GO; GO:0051096; P:positive regulation of helicase activity; IBA:GO_Central.
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   PIRSF; PIRSF002070; SSB; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00621; ssb; 1.
DR   PROSITE; PS50935; SSB; 1.
PE   3: Inferred from homology;
KW   DNA damage; DNA recombination; DNA repair; DNA replication; DNA-binding;
KW   Reference proteome.
FT   CHAIN           1..160
FT                   /note="Single-stranded DNA-binding protein 2"
FT                   /id="PRO_0000096061"
FT   DOMAIN          2..104
FT                   /note="SSB"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT   REGION          107..160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           155..160
FT                   /note="Important for interaction with partner proteins"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT   COMPBIAS        107..145
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   160 AA;  17838 MW;  F00E3DB01FA0D9A1 CRC64;
     MMNRVVLVGR LTKDPDLRYT PAGVAVATFT LAVNRTFTNQ NGEREADFIN CVVWRKPAEN
     VANFLKKGSM AGVDGRVQTR NYEDNDGKRV FVTEVVAESV QFLEPKNNNV EGATSNNYQN
     KANYSNNNQT SSYRADTSQK SDSFASEGKP IDINEDDLPF