ID   SURA_SALCH              Reviewed;         428 AA.
AC   Q57TG8;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=SCH_0087;
OS   Salmonella choleraesuis (strain SC-B67).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=321314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC-B67;
RX   PubMed=15781495; DOI=10.1093/nar/gki297;
RA   Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA   Lee Y.-S.;
RT   "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT   invasive and resistant zoonotic pathogen.";
RL   Nucleic Acids Res. 33:1690-1698(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; AE017220; AAX63993.1; -; Genomic_DNA.
DR   RefSeq; WP_011264182.1; NC_006905.1.
DR   AlphaFoldDB; Q57TG8; -.
DR   SMR; Q57TG8; -.
DR   EnsemblBacteria; AAX63993; AAX63993; SCH_0087.
DR   KEGG; sec:SCH_0087; -.
DR   HOGENOM; CLU_034646_11_0_6; -.
DR   OMA; EGGDMGW; -.
DR   Proteomes; UP000000538; 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; 2.
DR   PROSITE; PS50198; PPIC_PPIASE_2; 2.
PE   3: Inferred from homology;
KW   Chaperone; Isomerase; Periplasm; Repeat; Rotamase; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01183"
FT   CHAIN           21..428
FT                   /note="Chaperone SurA"
FT                   /id="PRO_0000270034"
FT   DOMAIN          171..272
FT                   /note="PpiC 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01183"
FT   DOMAIN          282..382
FT                   /note="PpiC 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01183"
SQ   SEQUENCE   428 AA;  47334 MW;  636177A01056F5C2 CRC64;
     MKNWKTLLLG IAMIANTSFA APQVVDKVAA IVNNGVVLES DVDGLMQSVK LNAGQAGQQL
     PDDATLRHQI LERLIMDQII LQMGQKMGVK ITDEQLDQAI ANIAKQNNMT MDQMRSRLAY
     DGLNYSTYRN QIRKEMIISE VRNNEVRRRI TVLPQEVDAL AKQIGTQNDA STELNLRHIL
     IALPENPTSE QVNDAQRQAE SIVEEARNGA DFGKLAITYS ADQQALKGGQ MGWGRIQELP
     GIFAQALSTA KKGDIVGPIR SGVGFHILKV NDLRGQSQSI SVTEVHARHI LLKPSPIMND
     QQARLKLEEI AADIKSGKTT FAAAAKEYSQ DPGSANQGGD LGWATPDIFD PAFRDALTKL
     HKGQISAPVH SSFGWHLIEL LDTRKVDKTD AAQKDRAYRM LMNRKFSEEA ATWMQEQRAS
     AYVKILSN