ID   SPY_ECOBD               Reviewed;         161 AA.
AC   C6ECL5; C5W4R8;
DT   16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Periplasmic chaperone Spy;
DE   AltName: Full=Spheroplast protein Y;
DE   Flags: Precursor;
GN   Name=spy; OrderedLocusNames=ECBD_1902;
OS   Escherichia coli (strain B / BL21-DE3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=469008;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B / BL21-DE3;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., LaButti K.M., Clum A., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Anderson I., Sorek R., Rubin E.;
RT   "Complete sequence of Escherichia coli BL21(DE3).";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 24-161, SUBUNIT, AND DOMAIN.
RC   STRAIN=B / BL21-DE3;
RX   PubMed=20799348; DOI=10.1002/pro.489;
RA   Kwon E., Kim D.Y., Gross C.A., Gross J.D., Kim K.K.;
RT   "The crystal structure Escherichia coli Spy.";
RL   Protein Sci. 19:2252-2259(2010).
CC   -!- FUNCTION: An ATP-independent periplasmic chaperone, decreases protein
CC       aggregation and helps protein refolding. Binds substrate over a large
CC       region. {ECO:0000250|UniProtKB:P77754}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20799348}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:P77754}.
CC   -!- DOMAIN: Has an elongated cradle shape. {ECO:0000269|PubMed:20799348}.
CC   -!- SIMILARITY: Belongs to the CpxP/Spy family. {ECO:0000305}.
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DR   EMBL; CP001665; ACT28949.1; -; Genomic_DNA.
DR   RefSeq; WP_001228987.1; NZ_CP053602.1.
DR   PDB; 3OEO; X-ray; 2.70 A; A/B/C/D=24-161.
DR   PDBsum; 3OEO; -.
DR   AlphaFoldDB; C6ECL5; -.
DR   SMR; C6ECL5; -.
DR   STRING; 469008.B21_01700; -.
DR   KEGG; ebd:ECBD_1902; -.
DR   PATRIC; fig|469008.15.peg.1733; -.
DR   eggNOG; COG3678; Bacteria.
DR   HOGENOM; CLU_124352_1_0_6; -.
DR   OMA; HDMMFKD; -.
DR   Proteomes; UP000002032; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   CDD; cd09916; CpxP_like; 1.
DR   DisProt; DP02077; -.
DR   InterPro; IPR012899; LTXXQ.
DR   Pfam; PF07813; LTXXQ; 1.
DR   PIRSF; PIRSF034445; CpxP_Spy; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chaperone; Periplasm; Signal; Stress response.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..161
FT                   /note="Periplasmic chaperone Spy"
FT                   /id="PRO_5002964807"
FT   REGION          140..161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   HELIX           61..72
FT                   /evidence="ECO:0007829|PDB:3OEO"
FT   STRAND          73..76
FT                   /evidence="ECO:0007829|PDB:3OEO"
FT   HELIX           83..91
FT                   /evidence="ECO:0007829|PDB:3OEO"
FT   HELIX           98..105
FT                   /evidence="ECO:0007829|PDB:3OEO"
FT   HELIX           106..108
FT                   /evidence="ECO:0007829|PDB:3OEO"
FT   HELIX           110..127
FT                   /evidence="ECO:0007829|PDB:3OEO"
FT   HELIX           132..141
FT                   /evidence="ECO:0007829|PDB:3OEO"
SQ   SEQUENCE   161 AA;  18229 MW;  A4623A967FD999CD CRC64;
     MRKLTALFVA STLALGAANL AHAADTTTAA PADAKPMMHH KGKFGPHQDM MFKDLNLTDA
     QKQQIREIMK GQRDQMKRPP LEERRAMHDI ITSDTFDKVK AEAQIAKMEE QRKANMLAHM
     ETQNKIYNIL TPEQKKQFNA NFEKRLTERP AAKGKMPATA E