ID   SURA_RALSO              Reviewed;         496 AA.
AC   Q8Y220;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 100.
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=RSc0516;
OS   Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=267608;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GMI1000;
RX   PubMed=11823852; DOI=10.1038/415497a;
RA   Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA   Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA   Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA   Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA   Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT   "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL   Nature 415:497-502(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. {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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAD14044.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AL646052; CAD14044.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_020831275.1; NC_003295.1.
DR   AlphaFoldDB; Q8Y220; -.
DR   SMR; Q8Y220; -.
DR   STRING; 267608.RSc0516; -.
DR   EnsemblBacteria; CAD14044; CAD14044; RSc0516.
DR   GeneID; 60500027; -.
DR   KEGG; rso:RSc0516; -.
DR   eggNOG; COG0760; Bacteria.
DR   HOGENOM; CLU_034646_11_0_4; -.
DR   OMA; EGGDMGW; -.
DR   Proteomes; UP000001436; 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; 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;
KW   Chaperone; Isomerase; Periplasm; Reference proteome; Repeat; Rotamase;
KW   Signal.
FT   SIGNAL          1..42
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01183"
FT   CHAIN           43..496
FT                   /note="Chaperone SurA"
FT                   /id="PRO_0000270033"
FT   DOMAIN          235..337
FT                   /note="PpiC 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01183"
FT   DOMAIN          349..447
FT                   /note="PpiC 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01183"
FT   REGION          53..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   496 AA;  53610 MW;  E91498C2D67312CC CRC64;
     MACKSTAVRS ATRVAPTRRL GMVTGALVAL MAGAALLPAA HAQQTQKKSA PLRGIFTTPD
     ASPSQPLLRG TLPGPSTASG AARSQLVDEV VAVVNTDIIT RRELLDRADL VERTLQSQNR
     QVPVRADLLG EVLEQLILER VQAQTAKESG IRVSDADVDR AVESVAQRNN LSVSQLKSKL
     AQSGLAYDKY REDLRQEILL ARLRDREVDS KVQVFDGEID NFLAQQGGSA ASSGVQEYNV
     AQILVPVAED ASAEQKAAAR GKAESLLKQV QGGADFAKLA RDSSGAPEAA QGGELGLRPI
     GRLPAQFANA VVDLKPGQVV DQVIESPAGF HVLKLVDKRA QGTAITAKVA QTQVRHILIK
     TGPTMSADDA RRQLAGLRDR IVHGYDFGDA ARRYSQDTSA SAGGELGWVS PGQLVPEFEQ
     AMGLLKPGEV SQPVQSQFGL HLIQVEGRRE AEVPVDRQRD YARSVIREQK VQAAYEDWLR
     QLRDSAHVEY RVNRQQ