SURA_ECOLI
ID SURA_ECOLI Reviewed; 428 AA.
AC P0ABZ6; P21202; P75630; Q8KIP6; Q8KMY0;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Chaperone SurA;
DE AltName: Full=Peptidyl-prolyl cis-trans isomerase SurA;
DE Short=PPIase SurA;
DE EC=5.2.1.8 {ECO:0000269|PubMed:8985185};
DE AltName: Full=Rotamase SurA;
DE AltName: Full=Survival protein A;
DE Flags: Precursor;
GN Name=surA; OrderedLocusNames=b0053, JW0052;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Almiron M., Tormo A., Kolter R.;
RL Unpublished observations (JAN-1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA Mizobuchi K., Nakata A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT 2.4 min region.";
RL Nucleic Acids Res. 20:3305-3308(1992).
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], AND SEQUENCE REVISION.
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 331-428.
RC STRAIN=K12;
RX PubMed=2670894; DOI=10.1128/jb.171.9.4767-4777.1989;
RA Roa B.B., Connolly D.M., Winkler M.E.;
RT "Overlap between pdxA and ksgA in the complex pdxA-ksgA-apaG-apaH operon of
RT Escherichia coli K-12.";
RL J. Bacteriol. 171:4767-4777(1989).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Abe S., Okutsu T., Negishi T., Nakajima H., Aono R.;
RT "N-hexane sensitivity of Escherichia coli due to low expression of ostA/imp
RT by insertion of IS2 and identification of the gene product as an outer
RT membrane protein.";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PROTEIN SEQUENCE OF 21-32.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [8]
RP PROTEIN SEQUENCE OF 21-30, AND CHARACTERIZATION.
RX PubMed=8626309; DOI=10.1128/jb.178.6.1770-1773.1996;
RA Lazar S.W., Kolter R.;
RT "SurA assists the folding of Escherichia coli outer membrane proteins.";
RL J. Bacteriol. 178:1770-1773(1996).
RN [9]
RP PROTEIN SEQUENCE OF 21-24.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9600841; DOI=10.1006/jmbi.1998.1726;
RA Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C.,
RA Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L.,
RA Hochstrasser D.F.;
RT "Protein identification with N and C-terminal sequence tags in proteome
RT projects.";
RL J. Mol. Biol. 278:599-608(1998).
RN [10]
RP FUNCTION.
RX PubMed=2165476; DOI=10.1128/jb.172.8.4339-4347.1990;
RA Tormo A., Almiron M., Kolter R.;
RT "surA, an Escherichia coli gene essential for survival in stationary
RT phase.";
RL J. Bacteriol. 172:4339-4347(1990).
RN [11]
RP CHARACTERIZATION.
RX PubMed=8878048; DOI=10.1046/j.1365-2958.1996.561412.x;
RA Missiakas D., Betton J.-M., Raina S.;
RT "New components of protein folding in extracytoplasmic compartments of
RT Escherichia coli SurA, FkpA and Skp/OmpH.";
RL Mol. Microbiol. 21:871-884(1996).
RN [12]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=8985185; DOI=10.1101/gad.10.24.3170;
RA Rouviere P.E., Gross C.A.;
RT "SurA, a periplasmic protein with peptidyl-prolyl isomerase activity,
RT participates in the assembly of outer membrane porins.";
RL Genes Dev. 10:3170-3182(1996).
RN [13]
RP DOMAIN FUNCTION.
RX PubMed=11226178; DOI=10.1093/emboj/20.1.285;
RA Behrens S., Maier R., de Cock H., Schmid F.X., Gross C.A.;
RT "The SurA periplasmic PPIase lacking its parvulin domains functions in vivo
RT and has chaperone activity.";
RL EMBO J. 20:285-294(2001).
RN [14]
RP SUBSTRATE RECOGNITION.
RX PubMed=14506253; DOI=10.1074/jbc.m308853200;
RA Bitto E., McKay D.B.;
RT "The periplasmic molecular chaperone protein SurA binds a peptide motif
RT that is characteristic of integral outer membrane proteins.";
RL J. Biol. Chem. 278:49316-49322(2003).
RN [15]
RP SUBSTRATE RECOGNITION.
RX PubMed=15840585; DOI=10.1074/jbc.m413742200;
RA Hennecke G., Nolte J., Volkmer-Engert R., Schneider-Mergener J.,
RA Behrens S.;
RT "The periplasmic chaperone SurA exploits two features characteristic of
RT integral outer membrane proteins for selective substrate recognition.";
RL J. Biol. Chem. 280:23540-23548(2005).
RN [16]
RP FUNCTION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=16267292; DOI=10.1128/jb.187.22.7680-7686.2005;
RA Justice S.S., Hunstad D.A., Harper J.R., Duguay A.R., Pinkner J.S.,
RA Bann J., Frieden C., Silhavy T.J., Hultgren S.J.;
RT "Periplasmic peptidyl prolyl cis-trans isomerases are not essential for
RT viability, but SurA is required for pilus biogenesis in Escherichia coli.";
RL J. Bacteriol. 187:7680-7686(2005).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 21-428.
RX PubMed=12429090; DOI=10.1016/s0969-2126(02)00877-8;
RA Bitto E., McKay D.B.;
RT "Crystallographic structure of SurA, a molecular chaperone that facilitates
RT folding of outer membrane porins.";
RL Structure 10:1489-1498(2002).
CC -!- FUNCTION: Chaperone involved in the correct folding and assembly of
CC outer membrane proteins, such as OmpA, OmpF and LamB (PubMed:8985185).
CC Recognizes specific patterns of aromatic residues and the orientation
CC of their side chains, which are found more frequently in integral outer
CC membrane proteins (PubMed:8985185). May act in both early periplasmic
CC and late outer membrane-associated steps of protein maturation
CC (PubMed:2165476). Essential for the survival of E.coli in stationary
CC phase. Required for pilus biogenesis (PubMed:16267292).
CC {ECO:0000269|PubMed:16267292, ECO:0000269|PubMed:2165476,
CC ECO:0000269|PubMed:8985185}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8; Evidence={ECO:0000269|PubMed:8985185};
CC -!- INTERACTION:
CC P0ABZ6; P77774: bamB; NbExp=2; IntAct=EBI-558651, EBI-907297;
CC -!- SUBCELLULAR LOCATION: Periplasm. Note=Is capable of associating with
CC the outer membrane.
CC -!- DOMAIN: The PPIase activity resides only in the second parvulin domain.
CC The N-terminal region and the C-terminal tail are necessary and
CC sufficient for the chaperone activity of SurA. The PPIase activity is
CC dispensable for SurA function as a SurA protein with a deletion of the
CC parvulin domains is almost completely functional in vivo. The N-
CC terminal region and the C-terminal tail are also required for porin
CC recognition. {ECO:0000269|PubMed:11226178}.
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DR EMBL; U00096; AAC73164.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96620.2; -; Genomic_DNA.
DR EMBL; M68521; AAA24304.1; -; Genomic_DNA.
DR EMBL; AB013134; BAA34131.1; -; Genomic_DNA.
DR PIR; E64726; E64726.
DR RefSeq; NP_414595.1; NC_000913.3.
DR RefSeq; WP_000800457.1; NZ_STEB01000010.1.
DR PDB; 1M5Y; X-ray; 3.00 A; A/B/C/D=21-428.
DR PDB; 2PV1; X-ray; 1.30 A; A=172-274.
DR PDB; 2PV2; X-ray; 1.30 A; A/B/C/D=172-274.
DR PDB; 2PV3; X-ray; 3.39 A; A/B=21-428.
DR PDBsum; 1M5Y; -.
DR PDBsum; 2PV1; -.
DR PDBsum; 2PV2; -.
DR PDBsum; 2PV3; -.
DR AlphaFoldDB; P0ABZ6; -.
DR SMR; P0ABZ6; -.
DR BioGRID; 4261014; 418.
DR DIP; DIP-35827N; -.
DR IntAct; P0ABZ6; 10.
DR STRING; 511145.b0053; -.
DR BindingDB; P0ABZ6; -.
DR ChEMBL; CHEMBL4295570; -.
DR SWISS-2DPAGE; P0ABZ6; -.
DR jPOST; P0ABZ6; -.
DR PaxDb; P0ABZ6; -.
DR PRIDE; P0ABZ6; -.
DR EnsemblBacteria; AAC73164; AAC73164; b0053.
DR EnsemblBacteria; BAB96620; BAB96620; BAB96620.
DR GeneID; 58460807; -.
DR GeneID; 944812; -.
DR KEGG; ecj:JW0052; -.
DR KEGG; eco:b0053; -.
DR PATRIC; fig|1411691.4.peg.2230; -.
DR EchoBASE; EB0978; -.
DR eggNOG; COG0760; Bacteria.
DR HOGENOM; CLU_034646_11_0_6; -.
DR InParanoid; P0ABZ6; -.
DR OMA; EGGDMGW; -.
DR PhylomeDB; P0ABZ6; -.
DR BioCyc; EcoCyc:EG10985-MON; -.
DR BioCyc; MetaCyc:EG10985-MON; -.
DR EvolutionaryTrace; P0ABZ6; -.
DR PRO; PR:P0ABZ6; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0042277; F:peptide binding; IEA:InterPro.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:EcoCyc.
DR GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IDA:EcoCyc.
DR GO; GO:0043165; P:Gram-negative-bacterium-type cell outer membrane assembly; IMP:EcoliWiki.
DR GO; GO:0060274; P:maintenance of stationary phase; IMP:EcoliWiki.
DR GO; GO:0036506; P:maintenance of unfolded protein; IDA:EcoCyc.
DR GO; GO:0006457; P:protein folding; IMP:EcoCyc.
DR GO; GO:0050821; P:protein stabilization; IMP:CACAO.
DR Gene3D; 3.10.50.40; -; 2.
DR HAMAP; MF_01183; Chaperone_SurA; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR000297; PPIase_PpiC.
DR InterPro; IPR023058; PPIase_PpiC_CS.
DR InterPro; IPR023034; PPIase_SurA.
DR InterPro; IPR015391; SurA_N.
DR InterPro; IPR027304; Trigger_fact/SurA_dom_sf.
DR Pfam; PF00639; Rotamase; 1.
DR Pfam; PF09312; SurA_N; 1.
DR SUPFAM; SSF109998; SSF109998; 1.
DR PROSITE; PS01096; PPIC_PPIASE_1; 2.
DR PROSITE; PS50198; PPIC_PPIASE_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Direct protein sequencing; Isomerase; Periplasm;
KW Reference proteome; Repeat; Rotamase; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:8626309,
FT ECO:0000269|PubMed:9298646, ECO:0000269|PubMed:9600841"
FT CHAIN 21..428
FT /note="Chaperone SurA"
FT /id="PRO_0000025542"
FT DOMAIN 171..272
FT /note="PpiC 1"
FT DOMAIN 282..382
FT /note="PpiC 2"
FT CONFLICT 25
FT /note="V -> D (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="S -> T (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="G -> GFG (in Ref. 1)"
FT /evidence="ECO:0000305"
FT STRAND 28..38
FT /evidence="ECO:0007829|PDB:1M5Y"
FT HELIX 39..54
FT /evidence="ECO:0007829|PDB:1M5Y"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:1M5Y"
FT HELIX 63..86
FT /evidence="ECO:0007829|PDB:1M5Y"
FT HELIX 93..106
FT /evidence="ECO:0007829|PDB:1M5Y"
FT HELIX 111..121
FT /evidence="ECO:0007829|PDB:1M5Y"
FT HELIX 125..148
FT /evidence="ECO:0007829|PDB:1M5Y"
FT HELIX 156..162
FT /evidence="ECO:0007829|PDB:1M5Y"
FT STRAND 173..182
FT /evidence="ECO:0007829|PDB:2PV1"
FT HELIX 189..207
FT /evidence="ECO:0007829|PDB:2PV1"
FT HELIX 212..219
FT /evidence="ECO:0007829|PDB:2PV1"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:2PV1"
FT STRAND 230..234
FT /evidence="ECO:0007829|PDB:2PV1"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:2PV1"
FT HELIX 241..246
FT /evidence="ECO:0007829|PDB:2PV1"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:2PV1"
FT STRAND 255..261
FT /evidence="ECO:0007829|PDB:2PV1"
FT STRAND 264..274
FT /evidence="ECO:0007829|PDB:2PV1"
FT STRAND 282..292
FT /evidence="ECO:0007829|PDB:1M5Y"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:1M5Y"
FT HELIX 300..315
FT /evidence="ECO:0007829|PDB:1M5Y"
FT HELIX 321..328
FT /evidence="ECO:0007829|PDB:1M5Y"
FT TURN 332..334
FT /evidence="ECO:0007829|PDB:1M5Y"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:1M5Y"
FT STRAND 340..344
FT /evidence="ECO:0007829|PDB:1M5Y"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:1M5Y"
FT HELIX 351..358
FT /evidence="ECO:0007829|PDB:1M5Y"
FT STRAND 375..386
FT /evidence="ECO:0007829|PDB:1M5Y"
FT HELIX 396..420
FT /evidence="ECO:0007829|PDB:1M5Y"
FT STRAND 423..425
FT /evidence="ECO:0007829|PDB:1M5Y"
SQ SEQUENCE 428 AA; 47284 MW; 25F6AD4B903CBD8E CRC64;
MKNWKTLLLG IAMIANTSFA APQVVDKVAA VVNNGVVLES DVDGLMQSVK LNAAQARQQL
PDDATLRHQI MERLIMDQII LQMGQKMGVK ISDEQLDQAI ANIAKQNNMT LDQMRSRLAY
DGLNYNTYRN QIRKEMIISE VRNNEVRRRI TILPQEVESL AQQVGNQNDA STELNLSHIL
IPLPENPTSD QVNEAESQAR AIVDQARNGA DFGKLAIAHS ADQQALNGGQ MGWGRIQELP
GIFAQALSTA KKGDIVGPIR SGVGFHILKV NDLRGESKNI SVTEVHARHI LLKPSPIMTD
EQARVKLEQI AADIKSGKTT FAAAAKEFSQ DPGSANQGGD LGWATPDIFD PAFRDALTRL
NKGQMSAPVH SSFGWHLIEL LDTRNVDKTD AAQKDRAYRM LMNRKFSEEA ASWMQEQRAS
AYVKILSN
