SPY_ECOLI
ID SPY_ECOLI Reviewed; 161 AA.
AC P77754;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Periplasmic chaperone Spy {ECO:0000303|PubMed:21317898};
DE AltName: Full=Spheroplast protein Y {ECO:0000303|PubMed:9068658};
DE Flags: Precursor;
GN Name=spy {ECO:0000303|PubMed:9068658}; OrderedLocusNames=b1743, JW1732;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 24-40, SUBCELLULAR
RP LOCATION, DEVELOPMENTAL STAGE, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC4100;
RX PubMed=9068658; DOI=10.1128/jb.179.6.2073-2076.1997;
RA Hagenmaier S., Stierhof Y.-D., Henning U.;
RT "A new periplasmic protein of Escherichia coli which is synthesized in
RT spheroplasts but not in intact cells.";
RL J. Bacteriol. 179:2073-2076(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 24-38, SUBCELLULAR LOCATION, AND INDUCTION BY ZINC.
RX PubMed=9694902; DOI=10.1074/jbc.273.33.21393;
RA Noll M., Petrukhin K., Lutsenko S.;
RT "Identification of a novel transcription regulator from Proteus mirabilis,
RT PMTR, revealed a possible role of YJAI protein in balancing zinc in
RT Escherichia coli.";
RL J. Biol. Chem. 273:21393-21401(1998).
RN [6]
RP INDUCTION BY CPX ENVELOPE STRESS RESPONSE, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC4100;
RX PubMed=10972835; DOI=10.1046/j.1365-2958.2000.02074.x;
RA Raivio T.L., Laird M.W., Joly J.C., Silhavy T.J.;
RT "Tethering of CpxP to the inner membrane prevents spheroplast induction of
RT the cpx envelope stress response.";
RL Mol. Microbiol. 37:1186-1197(2000).
RN [7]
RP INDUCTION BY BOTH BAE AND CXP ENVELOPE STRESS RESPONSES.
RC STRAIN=K12 / MC4100;
RX PubMed=12354228; DOI=10.1046/j.1365-2958.2002.03112.x;
RA Raffa R.G., Raivio T.L.;
RT "A third envelope stress signal transduction pathway in Escherichia coli.";
RL Mol. Microbiol. 45:1599-1611(2002).
RN [8]
RP FUNCTION, SUBSTRATE-BINDING, SUBCELLULAR LOCATION, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=21317898; DOI=10.1038/nsmb.2016;
RA Quan S., Koldewey P., Tapley T., Kirsch N., Ruane K.M., Pfizenmaier J.,
RA Shi R., Hofmann S., Foit L., Ren G., Jakob U., Xu Z., Cygler M.,
RA Bardwell J.C.;
RT "Genetic selection designed to stabilize proteins uncovers a chaperone
RT called Spy.";
RL Nat. Struct. Mol. Biol. 18:262-269(2011).
RN [9]
RP FUNCTION, SUBSTRATE-BINDING, AND MUTAGENESIS OF GLN-48; LEU-55; GLN-72;
RP HIS-119; GLN-123 AND PHE-138.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=24497545; DOI=10.7554/elife.01584;
RA Quan S., Wang L., Petrotchenko E.V., Makepeace K.A., Horowitz S., Yang J.,
RA Zhang Y., Borchers C.H., Bardwell J.C.;
RT "Super Spy variants implicate flexibility in chaperone action.";
RL Elife 3:E01584-E01584(2014).
RN [10]
RP INDUCTION.
RC STRAIN=K12 / BW25113;
RX PubMed=24999585; DOI=10.1016/j.gene.2014.07.003;
RA Srivastava S.K., Lambadi P.R., Ghosh T., Pathania R., Navani N.K.;
RT "Genetic regulation of spy gene expression in Escherichia coli in the
RT presence of protein unfolding agent ethanol.";
RL Gene 548:142-148(2014).
RN [11]
RP FUNCTION, AND REACTION MECHANISM.
RX PubMed=26619265; DOI=10.1038/nsmb.3133;
RA Stull F., Koldewey P., Humes J.R., Radford S.E., Bardwell J.C.;
RT "Substrate protein folds while it is bound to the ATP-independent chaperone
RT Spy.";
RL Nat. Struct. Mol. Biol. 23:53-58(2016).
CC -!- FUNCTION: An ATP-independent periplasmic chaperone, decreases protein
CC aggregation and helps protein refolding. Binds substrate over a large
CC region of its convex inner surface (PubMed:21317898, PubMed:24497545).
CC Substrate protein folds while it is bound to chaperone
CC (PubMed:26619265). Increasing Spy flexibility increases its substrate
CC affinity and overall chaperone activity (shown for 3 different
CC substrates) (PubMed:24497545). Protects proteins in vitro against
CC tannin inactivation; tannins have antimicrobial activity
CC (PubMed:21317898). Overexpression enhances the stability of otherwise
CC unstable periplasmic proteins (PubMed:21317898).
CC {ECO:0000269|PubMed:21317898, ECO:0000269|PubMed:24497545,
CC ECO:0000269|PubMed:26619265}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q8XDZ4}.
CC -!- INTERACTION:
CC P77754; Q03708: imm; Xeno; NbExp=2; IntAct=EBI-1121716, EBI-1035025;
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:21317898,
CC ECO:0000269|PubMed:9068658, ECO:0000269|PubMed:9694902}.
CC -!- DEVELOPMENTAL STAGE: Produced abundantly in spheroplasts, not detected
CC in intact cells. {ECO:0000269|PubMed:9068658}.
CC -!- INDUCTION: Induced by many sorts of periplasmic stress. Produced upon
CC spheroplast formation, not induced by growth in 0.5 M sucrose or 0.35 M
CC NaCl, nor by mutants that have a leaky periplasmic space (at protein
CC level) (PubMed:9068658). Induction is partially dependent on the Cpx
CC envelope stress response encoded by cpxA-cpxR; does not depend on sigma
CC factor E (rpoE) (PubMed:10972835). Induction is also partially
CC dependent on the Bae envelope stress response encoded by baeS-baeR; cpx
CC and baeS effects are independent (PubMed:12354228). Overexpression of P
CC pili protein PapG induces spy expression via both Cpx and Bae,
CC overexpression of outer membrane protein NlpE induces spy via only Cpx
CC whereas indole induces spy expression only via Bae (PubMed:12354228).
CC Induced by 1 mM zinc (at protein level) (PubMed:9694902), via Bae,
CC which also regulates ethanol induction of spy (PubMed:24999585).
CC Induced by copper via Cpx (PubMed:24999585). Induced by tannic acid (to
CC 25% of total periplasmic protein), butanol (to 20% total periplasmic
CC protein) and ethanol (to 5% total periplasmic protein) (at protein
CC level) (PubMed:21317898). {ECO:0000269|PubMed:10972835,
CC ECO:0000269|PubMed:12354228, ECO:0000269|PubMed:21317898,
CC ECO:0000269|PubMed:24999585, ECO:0000269|PubMed:9068658,
CC ECO:0000269|PubMed:9694902}.
CC -!- DOMAIN: Has an elongated cradle shape. {ECO:0000250|UniProtKB:Q8XDZ4,
CC ECO:0000305|PubMed:24497545}.
CC -!- DISRUPTION PHENOTYPE: No observed growth phenotype (PubMed:9068658).
CC Increased levels of degP and rpoH transcription; may induce the sigma
CC factor E regulon (rpoE) (PubMed:10972835). Loss of about 50% of
CC periplasmic alkaline phosphatase activity; very sensitive to tannic
CC acid (PubMed:21317898). {ECO:0000269|PubMed:10972835,
CC ECO:0000269|PubMed:21317898, ECO:0000269|PubMed:9068658}.
CC -!- SIMILARITY: Belongs to the CpxP/Spy family. {ECO:0000305}.
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DR EMBL; Y07714; CAA68986.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74813.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15531.1; -; Genomic_DNA.
DR PIR; G64933; G64933.
DR RefSeq; NP_416257.1; NC_000913.3.
DR RefSeq; WP_001228984.1; NZ_SSZK01000001.1.
DR PDB; 5WNW; X-ray; 1.79 A; A/B=52-147.
DR PDB; 5WO1; X-ray; 1.87 A; A/B=52-147.
DR PDB; 5WO2; X-ray; 1.77 A; A/B=52-147.
DR PDB; 5WO3; X-ray; 1.87 A; A/B=52-147.
DR PDB; 6BIE; X-ray; 1.77 A; A/B=52-147.
DR PDB; 6OWX; X-ray; 2.06 A; A/B=52-147.
DR PDB; 6OWY; X-ray; 2.07 A; A/B=52-147.
DR PDB; 6OWZ; X-ray; 2.05 A; A/B=52-147.
DR PDBsum; 5WNW; -.
DR PDBsum; 5WO1; -.
DR PDBsum; 5WO2; -.
DR PDBsum; 5WO3; -.
DR PDBsum; 6BIE; -.
DR PDBsum; 6OWX; -.
DR PDBsum; 6OWY; -.
DR PDBsum; 6OWZ; -.
DR AlphaFoldDB; P77754; -.
DR SMR; P77754; -.
DR BioGRID; 4262237; 147.
DR DIP; DIP-10914N; -.
DR IntAct; P77754; 4.
DR STRING; 511145.b1743; -.
DR jPOST; P77754; -.
DR PaxDb; P77754; -.
DR PRIDE; P77754; -.
DR EnsemblBacteria; AAC74813; AAC74813; b1743.
DR EnsemblBacteria; BAA15531; BAA15531; BAA15531.
DR GeneID; 946253; -.
DR KEGG; ecj:JW1732; -.
DR KEGG; eco:b1743; -.
DR PATRIC; fig|1411691.4.peg.513; -.
DR EchoBASE; EB3263; -.
DR eggNOG; COG3678; Bacteria.
DR HOGENOM; CLU_124352_1_0_6; -.
DR InParanoid; P77754; -.
DR OMA; HDMMFKD; -.
DR PhylomeDB; P77754; -.
DR BioCyc; EcoCyc:G6939-MON; -.
DR PRO; PR:P77754; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0044183; F:protein folding chaperone; IDA:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; IDA:EcoCyc.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IDA:EcoCyc.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:EcoCyc.
DR CDD; cd09916; CpxP_like; 1.
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; Direct protein sequencing; Periplasm;
KW Reference proteome; Signal; Stress response.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:9068658,
FT ECO:0000269|PubMed:9694902"
FT CHAIN 24..161
FT /note="Periplasmic chaperone Spy"
FT /id="PRO_0000022405"
FT REGION 140..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 48
FT /note="Q->R: Increased chaperone activity, substrate
FT affinity and chaperone flexibility."
FT /evidence="ECO:0000269|PubMed:24497545"
FT MUTAGEN 55
FT /note="L->P: Increased chaperone activity, substrate
FT affinity and chaperone flexibility."
FT /evidence="ECO:0000269|PubMed:24497545"
FT MUTAGEN 72
FT /note="Q->L: Increased chaperone activity, substrate
FT affinity and chaperone flexibility, despite decreased Spy
FT stability."
FT /evidence="ECO:0000269|PubMed:24497545"
FT MUTAGEN 119
FT /note="H->L: Increased chaperone activity, substrate
FT affinity and chaperone flexibility."
FT /evidence="ECO:0000269|PubMed:24497545"
FT MUTAGEN 123
FT /note="Q->L: Increased chaperone activity, substrate
FT affinity and chaperone flexibility."
FT /evidence="ECO:0000269|PubMed:24497545"
FT MUTAGEN 138
FT /note="F->I,L: Increased chaperone activity, substrate
FT affinity and chaperone flexibility."
FT /evidence="ECO:0000269|PubMed:24497545"
FT CONFLICT 38
FT /note="M -> MM (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:5WO2"
FT HELIX 59..69
FT /evidence="ECO:0007829|PDB:5WO2"
FT HELIX 81..91
FT /evidence="ECO:0007829|PDB:5WO2"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:5WO2"
FT HELIX 98..106
FT /evidence="ECO:0007829|PDB:5WO2"
FT HELIX 109..127
FT /evidence="ECO:0007829|PDB:5WO2"
FT HELIX 132..143
FT /evidence="ECO:0007829|PDB:5WO2"
SQ SEQUENCE 161 AA; 18199 MW; B4733B967FC5F5BD CRC64;
MRKLTALFVA STLALGAANL AHAADTTTAA PADAKPMMHH KGKFGPHQDM MFKDLNLTDA
QKQQIREIMK GQRDQMKRPP LEERRAMHDI IASDTFDKVK AEAQIAKMEE QRKANMLAHM
ETQNKIYNIL TPEQKKQFNA NFEKRLTERP AAKGKMPATA E
