ID   SURA_BURTA              Reviewed;         448 AA.
AC   Q2T116;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Chaperone SurA {ECO:0000255|HAMAP-Rule:MF_01183};
DE   AltName: Full=Peptidyl-prolyl cis-trans isomerase SurA {ECO:0000255|HAMAP-Rule:MF_01183};
DE            Short=PPIase SurA {ECO:0000255|HAMAP-Rule:MF_01183};
DE            EC=5.2.1.8 {ECO:0000255|HAMAP-Rule:MF_01183};
DE   AltName: Full=Rotamase SurA {ECO:0000255|HAMAP-Rule:MF_01183};
DE   Flags: Precursor;
GN   Name=surA {ECO:0000255|HAMAP-Rule:MF_01183}; OrderedLocusNames=BTH_I0576;
OS   Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS   E264).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX   PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA   Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA   DeShazer D.;
RT   "Bacterial genome adaptation to niches: divergence of the potential
RT   virulence genes in three Burkholderia species of different survival
RT   strategies.";
RL   BMC Genomics 6:174-174(2005).
CC   -!- FUNCTION: Chaperone involved in the correct folding and assembly of
CC       outer membrane proteins. Recognizes specific patterns of aromatic
CC       residues and the orientation of their side chains, which are found more
CC       frequently in integral outer membrane proteins. May act in both early
CC       periplasmic and late outer membrane-associated steps of protein
CC       maturation. {ECO:0000255|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:0000255|HAMAP-
CC         Rule:MF_01183};
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_01183}.
CC       Note=Is capable of associating with the outer membrane.
CC       {ECO:0000255|HAMAP-Rule:MF_01183}.
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 to function as a chaperone. The N-terminal region
CC       and the C-terminal tail are also required for porin recognition.
CC       {ECO:0000255|HAMAP-Rule:MF_01183}.
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DR   EMBL; CP000086; ABC38226.1; -; Genomic_DNA.
DR   RefSeq; WP_009892911.1; NZ_CP008785.1.
DR   AlphaFoldDB; Q2T116; -.
DR   SMR; Q2T116; -.
DR   PRIDE; Q2T116; -.
DR   EnsemblBacteria; ABC38226; ABC38226; BTH_I0576.
DR   KEGG; bte:BTH_I0576; -.
DR   HOGENOM; CLU_034646_11_0_4; -.
DR   OMA; EGGDMGW; -.
DR   OrthoDB; 1838755at2; -.
DR   Proteomes; UP000001930; Chromosome I.
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:0006457; P:protein folding; IEA:UniProtKB-UniRule.
DR   GO; GO:0050821; P:protein stabilization; IEA:InterPro.
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; IPR023034; PPIase_SurA.
DR   InterPro; IPR015391; SurA_N.
DR   InterPro; IPR027304; Trigger_fact/SurA_dom_sf.
DR   Pfam; PF09312; SurA_N; 1.
DR   SUPFAM; SSF109998; SSF109998; 1.
DR   PROSITE; PS50198; PPIC_PPIASE_2; 2.
PE   3: Inferred from homology;
KW   Chaperone; Isomerase; Periplasm; Repeat; Rotamase; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01183"
FT   CHAIN           28..448
FT                   /note="Chaperone SurA"
FT                   /id="PRO_0000270009"
FT   DOMAIN          185..288
FT                   /note="PpiC 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01183"
FT   DOMAIN          301..399
FT                   /note="PpiC 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01183"
FT   REGION          230..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   448 AA;  48799 MW;  C87A0B5152A8F81D CRC64;
     MKKTLRFAAV AAGLVASLIT VAPSASAQAL RAQGASLADE VVAVVNNDVI TGRELDQRVG
     LIARRLQQQK APVPPTDQLR AQVLNQMVLE RIQVQRAKDD GIVVDNATVQ ATLGRLAQAN
     GMPLDQYKAR IEAQGVPWDL FVRDARTELM LSKLREKEVD SKITVSDAEV ASYIASQRGP
     NAGAQQDLRL EHIFVKAPTN APQADIDAAQ KKAEGLLQQA LASGTNFERL AKSQSEADDA
     KKGGDLGFKA PSSLPSDVVD AVSKLRPGEV NPTLIRVPDG FEIVRLVDRR ASQNPAASPK
     IVQTHVRHIL LRVGEGKSES QARQQLIDIR RQIEAGGDFE KFARTYSQDG SASQGGDLGW
     ISPGETVPEF ERAMNALQDG QVSNPVRTEY GYHLIQVLGR RDAEGSVQQQ MDIARQAIGQ
     RKAEQAYSDW LRELRDSSYV QIKLPVGQ