ID   SURA_BUCAP              Reviewed;         432 AA.
AC   Q8KA01;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=BUsg_133;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
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; AE013218; AAM67701.1; -; Genomic_DNA.
DR   RefSeq; WP_011053668.1; NC_004061.1.
DR   AlphaFoldDB; Q8KA01; -.
DR   SMR; Q8KA01; -.
DR   STRING; 198804.BUsg_133; -.
DR   PRIDE; Q8KA01; -.
DR   EnsemblBacteria; AAM67701; AAM67701; BUsg_133.
DR   KEGG; bas:BUsg_133; -.
DR   eggNOG; COG0760; Bacteria.
DR   HOGENOM; CLU_034646_11_0_6; -.
DR   OMA; EGGDMGW; -.
DR   OrthoDB; 1838755at2; -.
DR   Proteomes; UP000000416; 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; -; 1.
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; 1.
PE   3: Inferred from homology;
KW   Chaperone; Isomerase; Periplasm; Repeat; Rotamase; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..432
FT                   /note="Chaperone SurA"
FT                   /id="PRO_0000025541"
FT   DOMAIN          175..276
FT                   /note="PpiC 1"
FT   DOMAIN          286..386
FT                   /note="PpiC 2"
SQ   SEQUENCE   432 AA;  51748 MW;  698284DB452257ED CRC64;
     MKVYFFLILY VFLSFFSITY SKELEIDKII AIVNNQIILN SDVNQVLFSL KEEDQRVKIP
     LKINFLRNKI IKKLITETLI LEEAKKFNIV VTDDQVNNVL SKYALKKNIT IEELKRNILM
     NNTNTSFSYN DYFNKIKNSL KVKIIQDYVL HNRVHISEKE VDLFLNKLIN TQNELKKIDI
     NCIFLPFIKE KNKIFIKNTK ILADHFAKKI KKDASFNYYY EYFKKNNNIF LSKEIRSKSL
     KYLKKIFLNK LKIIKKNQIL GPILGLKGFY ILKINKIENE NKENLTTEFH IQHCLIRPSV
     ILDDKQAKNS IYYIYNNIKN KKYSFDYAVQ KLSHDVYSSH KKGDLGWIST DFFSNDFRNF
     LTDLRKNEIS KPIKSNFGWH IIKLLDIRQV DKSNRIDKNL VYRFLLEKKI KKERYNWIRQ
     LKKSSYIKIF KN