ID   SURA_PSEA6              Reviewed;         431 AA.
AC   Q15QB3;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=Patl_3419;
OS   Pseudoalteromonas atlantica (strain T6c / ATCC BAA-1087).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=342610;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T6c / ATCC BAA-1087;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Karls A.C.,
RA   Bartlett D., Higgins B.P., Richardson P.;
RT   "Complete sequence of Pseudoalteromonas atlantica T6c.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000388; ABG41925.1; -; Genomic_DNA.
DR   RefSeq; WP_011576154.1; NC_008228.1.
DR   AlphaFoldDB; Q15QB3; -.
DR   SMR; Q15QB3; -.
DR   STRING; 342610.Patl_3419; -.
DR   EnsemblBacteria; ABG41925; ABG41925; Patl_3419.
DR   KEGG; pat:Patl_3419; -.
DR   eggNOG; COG0760; Bacteria.
DR   HOGENOM; CLU_034646_11_0_6; -.
DR   OMA; EGGDMGW; -.
DR   OrthoDB; 1838755at2; -.
DR   Proteomes; UP000001981; 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; 2.
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..20
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01183"
FT   CHAIN           21..431
FT                   /note="Chaperone SurA"
FT                   /id="PRO_5000125744"
FT   DOMAIN          171..272
FT                   /note="PpiC 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01183"
FT   DOMAIN          281..381
FT                   /note="PpiC 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01183"
SQ   SEQUENCE   431 AA;  48219 MW;  4AD563DBEAADB45A CRC64;
     MKLTVVTFAL LAFISFNTFA KQVRLDNVAV IVDQGVVLES QIEELVNTVK RNALTNNQTL
     PSDRVLRTQA IERLIVDSLQ NQMAERMGIQ ISDPQLDQTI DNIAREDGTT VEDLRKNLAS
     EGVSFEVYRE QVRKELVTGE VRRANVRRRI YITPQEISNL VTLIDEQGGQ QAEYHLGHIL
     IGFPPEPTDE DVSKAKDTAE KVLELLNNGS EFAKIATASS SGSKALEGGD LGWMNINSMP
     TLFAEAVQGT SKDDLIGPIR SGAGFHVLKI IDFRGIEKVE VAELKSRHIL IKPSVILSDE
     KAEKMLTEFR KELLAGEADF AELAKEHSAD PGSALRGGDL GWADPNVYVP AFRDTLQSLE
     VGEISQPVRS THGWHLMQLM DKRVQDATEK RKEDKAYQLL FQRKFAEETE AWLKEMRDSA
     YVELLDEKDN S