PRIB_BORPE
ID PRIB_BORPE Reviewed; 107 AA.
AC P67673; Q7VV90; Q7W7P7; Q7WL34;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Primosomal replication protein N {ECO:0000255|HAMAP-Rule:MF_00720};
GN Name=priB {ECO:0000255|HAMAP-Rule:MF_00720}; OrderedLocusNames=BP2795;
OS Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257313;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
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; BX640419; CAE43068.1; -; Genomic_DNA.
DR RefSeq; NP_881395.1; NC_002929.2.
DR RefSeq; WP_003813095.1; NZ_CP039022.1.
DR PDB; 3KLW; X-ray; 2.00 A; A/B=1-98.
DR PDBsum; 3KLW; -.
DR AlphaFoldDB; P67673; -.
DR SMR; P67673; -.
DR STRING; 257313.BP2795; -.
DR GeneID; 56478075; -.
DR GeneID; 66438154; -.
DR KEGG; bpe:BP2795; -.
DR PATRIC; fig|257313.5.peg.3015; -.
DR eggNOG; COG2965; Bacteria.
DR HOGENOM; CLU_166075_1_2_4; -.
DR OMA; LLDCEGF; -.
DR EvolutionaryTrace; P67673; -.
DR Proteomes; UP000002676; 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; Reference proteome.
FT CHAIN 1..107
FT /note="Primosomal replication protein N"
FT /id="PRO_0000199047"
FT DOMAIN 1..97
FT /note="SSB"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00720"
FT STRAND 2..13
FT /evidence="ECO:0007829|PDB:3KLW"
FT STRAND 24..38
FT /evidence="ECO:0007829|PDB:3KLW"
FT STRAND 41..54
FT /evidence="ECO:0007829|PDB:3KLW"
FT HELIX 56..61
FT /evidence="ECO:0007829|PDB:3KLW"
FT STRAND 69..80
FT /evidence="ECO:0007829|PDB:3KLW"
FT STRAND 86..96
FT /evidence="ECO:0007829|PDB:3KLW"
SQ SEQUENCE 107 AA; 11424 MW; 58C63C068DC43904 CRC64;
MNTLELSARV LECGAMRHTP AGLPALELLL VHESEVVEAG HPRRVELTIS AVALGDLALL
LADTPLGTEM QVQGFLAPAR KDSVKVKLHL QQARRIAGSM GRDPLVG