SURA_PSEPK
ID SURA_PSEPK Reviewed; 427 AA.
AC Q88QT4;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 98.
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=PP_0403;
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(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=AAN66034.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE015451; AAN66034.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_742570.1; NC_002947.4.
DR AlphaFoldDB; Q88QT4; -.
DR SMR; Q88QT4; -.
DR STRING; 160488.PP_0403; -.
DR EnsemblBacteria; AAN66034; AAN66034; PP_0403.
DR KEGG; ppu:PP_0403; -.
DR PATRIC; fig|160488.4.peg.433; -.
DR eggNOG; COG0760; Bacteria.
DR HOGENOM; CLU_034646_11_0_6; -.
DR OMA; EGGDMGW; -.
DR PhylomeDB; Q88QT4; -.
DR Proteomes; UP000000556; 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..13
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01183"
FT CHAIN 14..427
FT /note="Chaperone SurA"
FT /id="PRO_0000270029"
FT DOMAIN 164..265
FT /note="PpiC 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01183"
FT DOMAIN 275..374
FT /note="PpiC 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01183"
SQ SEQUENCE 427 AA; 47649 MW; 621DAABD0837A70A CRC64;
MLGVALLSGA VHAAVQPLDR VVAIVDNDVV MQSQLDQRVH EVQQTIAKRG GGVPPTSALE
QQVLERLIVE NLQLQIGERS GIRITDEELN QAIGTIAQRN GMSLDQFRAA LARDGLSFDD
AREQVKREMI ISRVRQRRVA ERIQVSEQEV KNFLASDLGK MQMSEEYRLA NILIPTPEAA
NSDDIQKAAR KVGDVYQQLR QGADFGQMAI ANSASENALE GGEMGWRKAG QLPPDFAKML
SSMPVGEITQ PIRIPNGFII LKLEEKRGGS ENVLRDEVHV RHILIKPSEI RSEAATEQLA
ERLYDRIKNG EDFGELAKSF SEDPGSALNG GDLNWVDPNS LVPEFREQMA NAQQGVVTKP
FKTQYGWHVL EVLGRRATDS TEQAREQQAL SVLRNRKYDE ELQTWLRQIR DEAYVEIKLP
GADQAAQ
