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   27-MAR-2024, entry version 140.
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; Pseudomonadota; 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RL   Unpublished observations (JAN-1993).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
RT   0-2.4 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   jPOST; P0ABZ6; -.
DR   PaxDb; 511145-b0053; -.
DR   EnsemblBacteria; AAC73164; AAC73164; b0053.
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; HGWHIVQ; -.
DR   OrthoDB; 14196at2; -.
DR   PhylomeDB; P0ABZ6; -.
DR   BioCyc; EcoCyc:EG10985-MONOMER; -.
DR   BioCyc; MetaCyc:EG10985-MONOMER; -.
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; IPI:EcoCyc.
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   Gene3D; 1.10.4030.10; Porin chaperone SurA, peptide-binding domain; 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   PANTHER; PTHR47637; CHAPERONE SURA; 1.
DR   PANTHER; PTHR47637:SF1; CHAPERONE SURA; 1.
DR   Pfam; PF00639; Rotamase; 1.
DR   Pfam; PF13616; Rotamase_3; 1.
DR   Pfam; PF09312; SurA_N; 1.
DR   SUPFAM; SSF54534; FKBP-like; 2.
DR   SUPFAM; SSF109998; Triger factor/SurA peptide-binding domain-like; 1.
DR   PROSITE; PS01096; PPIC_PPIASE_1; 2.
DR   PROSITE; PS50198; PPIC_PPIASE_2; 2.
DR   SWISS-2DPAGE; P0ABZ6; -.
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
//