(data stored in SCRATCH zone)

SWISSPROT: B7UIA1_ECO27

ID   B7UIA1_ECO27            Unreviewed;       428 AA.
AC   B7UIA1;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 72.
DE   RecName: Full=Chaperone SurA {ECO:0000256|HAMAP-Rule:MF_01183};
DE   AltName: Full=Peptidyl-prolyl cis-trans isomerase SurA {ECO:0000256|HAMAP-Rule:MF_01183};
DE            Short=PPIase SurA {ECO:0000256|HAMAP-Rule:MF_01183};
DE            EC=5.2.1.8 {ECO:0000256|HAMAP-Rule:MF_01183};
DE   AltName: Full=Rotamase SurA {ECO:0000256|HAMAP-Rule:MF_01183};
DE   Flags: Precursor;
GN   Name=surA {ECO:0000256|HAMAP-Rule:MF_01183,
GN   ECO:0000313|EMBL:CAS07604.1};
GN   OrderedLocusNames=E2348C_0056 {ECO:0000313|EMBL:CAS07604.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS07604.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS07604.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- FUNCTION: Chaperone involved in the correct folding and assembly
CC       of outer membrane proteins. Recognizes specific patterns of
CC       aromatic residues and the orientation of their side chains, which
CC       are found more frequently in integral outer membrane proteins. May
CC       act in both early periplasmic and late outer membrane-associated
CC       steps of protein maturation. {ECO:0000256|HAMAP-Rule:MF_01183}.
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:0000256|HAMAP-
CC         Rule:MF_01183, ECO:0000256|SAAS:SAAS01128631};
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|HAMAP-Rule:MF_01183}.
CC       Note=Is capable of associating with the outer membrane.
CC       {ECO:0000256|HAMAP-Rule:MF_01183}.
CC   -!- DOMAIN: The PPIase activity resides only in the second parvulin
CC       domain. The N-terminal region and the C-terminal tail are
CC       necessary and sufficient for the chaperone activity of SurA. The
CC       PPIase activity is dispensable for SurA to function as a
CC       chaperone. The N-terminal region and the C-terminal tail are also
CC       required for porin recognition. {ECO:0000256|HAMAP-Rule:MF_01183}.
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DR   EMBL; FM180568; CAS07604.1; -; Genomic_DNA.
DR   RefSeq; WP_000800457.1; NC_011601.1.
DR   SMR; B7UIA1; -.
DR   EnsemblBacteria; CAS07604; CAS07604; E2348C_0056.
DR   KEGG; ecg:E2348C_0056; -.
DR   HOGENOM; HOG000264337; -.
DR   KO; K03771; -.
DR   OMA; EGGDMGW; -.
DR   BioCyc; ECOL574521:E2348C_RS00290-MONOMER; -.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0042277; F:peptide binding; IEA:InterPro.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0043165; P:Gram-negative-bacterium-type cell outer membrane assembly; IEA:InterPro.
DR   GO; GO:0060274; P:maintenance of stationary phase; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
DR   GO; GO:0050821; P:protein stabilization; IEA:InterPro.
DR   HAMAP; MF_01183; Chaperone_SurA; 1.
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; 1.
DR   PROSITE; PS50198; PPIC_PPIASE_2; 2.
PE   3: Inferred from homology;
DR   PRODOM; B7UIA1.
DR   SWISS-2DPAGE; B7UIA1.
KW   Chaperone {ECO:0000256|HAMAP-Rule:MF_01183,
KW   ECO:0000256|SAAS:SAAS00143314};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01183, ECO:0000256|PROSITE-
KW   ProRule:PRU00278, ECO:0000256|SAAS:SAAS00143328,
KW   ECO:0000313|EMBL:CAS07604.1};
KW   Periplasm {ECO:0000256|HAMAP-Rule:MF_01183};
KW   Repeat {ECO:0000256|HAMAP-Rule:MF_01183,
KW   ECO:0000256|SAAS:SAAS00015058};
KW   Rotamase {ECO:0000256|HAMAP-Rule:MF_01183, ECO:0000256|PROSITE-
KW   ProRule:PRU00278, ECO:0000256|SAAS:SAAS00143327};
KW   Signal {ECO:0000256|HAMAP-Rule:MF_01183}.
FT   SIGNAL        1     20       {ECO:0000256|HAMAP-Rule:MF_01183}.
FT   CHAIN        21    428       Chaperone SurA. {ECO:0000256|HAMAP-Rule:
FT                                MF_01183}.
FT                                /FTId=PRO_5009008041.
FT   DOMAIN      171    272       PpiC. {ECO:0000259|PROSITE:PS50198}.
FT   DOMAIN      282    382       PpiC. {ECO:0000259|PROSITE:PS50198}.
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
//

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