ID   SURA_BUCAI              Reviewed;         430 AA.
AC   P57240;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Chaperone SurA;
DE   AltName: Full=Peptidyl-prolyl cis-trans isomerase SurA;
DE            Short=PPIase SurA;
DE            EC=5.2.1.8;
DE   AltName: Full=Rotamase SurA;
DE   Flags: Precursor;
GN   Name=surA; OrderedLocusNames=BU140;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
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 (By similarity). {ECO:0000250}.
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;
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}. Note=Is capable of
CC       associating with the outer membrane. {ECO:0000250}.
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 (By
CC       similarity). {ECO:0000250}.
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DR   EMBL; BA000003; BAB12858.1; -; Genomic_DNA.
DR   RefSeq; NP_239972.1; NC_002528.1.
DR   RefSeq; WP_010895967.1; NC_002528.1.
DR   AlphaFoldDB; P57240; -.
DR   SMR; P57240; -.
DR   STRING; 107806.10038823; -.
DR   EnsemblBacteria; BAB12858; BAB12858; BAB12858.
DR   KEGG; buc:BU140; -.
DR   PATRIC; fig|107806.10.peg.149; -.
DR   eggNOG; COG0760; Bacteria.
DR   HOGENOM; CLU_034646_11_0_6; -.
DR   OMA; EGGDMGW; -.
DR   Proteomes; UP000001806; 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: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; PF00639; Rotamase; 1.
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; Reference proteome; Repeat; Rotamase;
KW   Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..430
FT                   /note="Chaperone SurA"
FT                   /id="PRO_0000025540"
FT   DOMAIN          174..275
FT                   /note="PpiC 1"
FT   DOMAIN          284..384
FT                   /note="PpiC 2"
SQ   SEQUENCE   430 AA;  50738 MW;  CA4C425B3FBA5788 CRC64;
     MKICIFIFFY IFSSIFYVLA KNNQVDNITA IVNDEIILNS DVNEILVFLK KSKKKFIIPL
     KSDFLKEKVL EKLIVDSLIL QEANSKNINI TKEQIDTVIK NIALKKHISV DHFKKQILLR
     NIKNPSYYDN FIKKIEILLK MKTIQDYELH KRINISEQEV NTIFKKLIKD NEKFKKINLS
     YILLPSLKQD SDNAVRNRTK IAENIVYKLK KGYDFEKLLI ECEKNKSTFI VKKMFWKPLL
     DIQNSFFKTL NIFKKGQILG PIVGDKGLYI LKVNDIHHKK ENIVTEFYMQ HCLIKPSVIL
     TNTEAKKKIF NIYENIKKGI YTFDDAVKNL SDDYYSSNKK GDLGWISKES LGFDLNKKFL
     ILDKNEISEP VKSNWGWHIF KILDRRQVDA FYKLKKNQAF NIVLNQKIIS EKNHWIEDLK
     NTAYIEIIRS