PRIB_BORPA
ID PRIB_BORPA Reviewed; 107 AA.
AC P67675; Q7VV90; Q7W7P7; Q7WL34;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Primosomal replication protein N {ECO:0000255|HAMAP-Rule:MF_00720};
GN Name=priB {ECO:0000255|HAMAP-Rule:MF_00720}; OrderedLocusNames=BPP2467;
OS Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257311;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12822 / ATCC BAA-587 / NCTC 13253;
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(2003).
CC -!- FUNCTION: Binds single-stranded DNA at the primosome assembly site
CC (PAS). {ECO:0000255|HAMAP-Rule:MF_00720}.
CC -!- SUBUNIT: Component of the preprimosomal complex composed of PriA, PriB,
CC PriC, DnaB and DnaT. Upon transient interaction with DnaG it forms the
CC primosome. {ECO:0000255|HAMAP-Rule:MF_00720}.
CC -!- SIMILARITY: Belongs to the PriB family. {ECO:0000255|HAMAP-
CC Rule:MF_00720}.
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DR EMBL; BX640430; CAE37762.1; -; Genomic_DNA.
DR RefSeq; WP_003813095.1; NC_002928.3.
DR PDB; 3FHW; X-ray; 1.90 A; A/B=1-107.
DR PDBsum; 3FHW; -.
DR AlphaFoldDB; P67675; -.
DR SMR; P67675; -.
DR EnsemblBacteria; CAE37762; CAE37762; BPP2467.
DR GeneID; 56478075; -.
DR GeneID; 66438154; -.
DR KEGG; bpa:BPP2467; -.
DR HOGENOM; CLU_166075_1_2_4; -.
DR OMA; LLDCEGF; -.
DR EvolutionaryTrace; P67675; -.
DR Proteomes; UP000001421; Chromosome.
DR GO; GO:1990077; C:primosome complex; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IEA:UniProtKB-KW.
DR Gene3D; 2.40.50.140; -; 1.
DR HAMAP; MF_00720; PriB; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR000424; Primosome_PriB/ssb.
DR InterPro; IPR023646; Prisomal_replication_PriB.
DR PIRSF; PIRSF003135; Primosomal_n; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR04418; PriB_gamma; 1.
DR PROSITE; PS50935; SSB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA replication; DNA-binding; Primosome.
FT CHAIN 1..107
FT /note="Primosomal replication protein N"
FT /id="PRO_0000199049"
FT DOMAIN 1..97
FT /note="SSB"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00720"
FT STRAND 2..13
FT /evidence="ECO:0007829|PDB:3FHW"
FT STRAND 24..35
FT /evidence="ECO:0007829|PDB:3FHW"
FT STRAND 44..54
FT /evidence="ECO:0007829|PDB:3FHW"
FT HELIX 56..61
FT /evidence="ECO:0007829|PDB:3FHW"
FT STRAND 69..80
FT /evidence="ECO:0007829|PDB:3FHW"
FT STRAND 84..95
FT /evidence="ECO:0007829|PDB:3FHW"
SQ SEQUENCE 107 AA; 11424 MW; 58C63C068DC43904 CRC64;
MNTLELSARV LECGAMRHTP AGLPALELLL VHESEVVEAG HPRRVELTIS AVALGDLALL
LADTPLGTEM QVQGFLAPAR KDSVKVKLHL QQARRIAGSM GRDPLVG
