ID   PSAB_YERPS              Reviewed;         273 AA.
AC   P69966; P31523; Q56979; Q66CR7;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Chaperone protein PsaB;
DE   Flags: Precursor;
GN   Name=psaB; OrderedLocusNames=YPTB1335;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=YPIII / Serotype O:3;
RX   PubMed=8698470; DOI=10.1128/iai.64.7.2483-2489.1996;
RA   Yang Y., Merriam J.J., Mueller J.P., Isberg R.R.;
RT   "The psa locus is responsible for thermoinducible binding of Yersinia
RT   pseudotuberculosis to cultured cells.";
RL   Infect. Immun. 64:2483-2489(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
CC   -!- FUNCTION: Required for the biogenesis of the pH 6 antigen.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the periplasmic pilus chaperone family.
CC       {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-23 is the initiator.
CC       {ECO:0000305}.
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; L76301; AAC37057.1; -; Genomic_DNA.
DR   EMBL; BX936398; CAH20575.1; -; Genomic_DNA.
DR   RefSeq; WP_002208793.1; NZ_CP009712.1.
DR   AlphaFoldDB; P69966; -.
DR   SMR; P69966; -.
DR   EnsemblBacteria; CAH20575; CAH20575; YPTB1335.
DR   GeneID; 66842231; -.
DR   KEGG; yps:YPTB1335; -.
DR   OMA; FMVMPPL; -.
DR   Proteomes; UP000001011; Chromosome.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:InterPro.
DR   GO; GO:0061077; P:chaperone-mediated protein folding; IEA:InterPro.
DR   Gene3D; 2.60.40.10; -; 2.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR008962; PapD-like_sf.
DR   InterPro; IPR036316; Pili_assmbl_chap_C_dom_sf.
DR   InterPro; IPR001829; Pili_assmbl_chaperone_bac.
DR   InterPro; IPR016148; Pili_assmbl_chaperone_C.
DR   InterPro; IPR018046; Pili_assmbl_chaperone_CS.
DR   InterPro; IPR016147; Pili_assmbl_chaperone_N.
DR   Pfam; PF02753; PapD_C; 1.
DR   Pfam; PF00345; PapD_N; 1.
DR   PRINTS; PR00969; CHAPERONPILI.
DR   SUPFAM; SSF49354; SSF49354; 1.
DR   SUPFAM; SSF49584; SSF49584; 1.
DR   PROSITE; PS00635; PILI_CHAPERONE; 1.
PE   3: Inferred from homology;
KW   Chaperone; Disulfide bond; Immunoglobulin domain; Periplasm; Signal.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..273
FT                   /note="Chaperone protein PsaB"
FT                   /id="PRO_0000009288"
FT   DISULFID        128..163
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   273 AA;  30648 MW;  E6FA6E03C4CA655C CRC64;
     MKNLFFSAYK KVFSYITSIV IFMVSLPYAY SQDVVVNTTK HLFTVKIGTT RVIYPSSSTK
     GVSVSVANPQ DYPILVQTQV KDEDKTSPAP FIVTPPLFRL DAGLQGRVRI IRTGGKFPED
     RETLQWLCLT GIPPKNGDAW GNTQNNPKNS SPTMDIQMSI STCIKLLFRP DKVKGDPTDS
     ADSLTWRYKG NYLEVNNPTP FYMNFYSLRI GDEKINLSDL GSKDEIKNGS YVPPFSSRDF
     IIPVKNKGKA TEVFWQVIND NGGVSREFKS TVQ