SURA_YERPE
ID SURA_YERPE Reviewed; 434 AA.
AC Q7CG87; Q74Q29;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
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};
GN OrderedLocusNames=YPO0494, y3681, YP_3685;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
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; AE009952; AAM87229.1; -; Genomic_DNA.
DR EMBL; AL590842; CAL19174.1; -; Genomic_DNA.
DR EMBL; AE017042; AAS63833.1; -; Genomic_DNA.
DR PIR; AD0061; AD0061.
DR RefSeq; WP_002210488.1; NZ_WUCM01000024.1.
DR RefSeq; YP_002345567.1; NC_003143.1.
DR AlphaFoldDB; Q7CG87; -.
DR SMR; Q7CG87; -.
DR IntAct; Q7CG87; 1.
DR STRING; 214092.YPO0494; -.
DR PaxDb; Q7CG87; -.
DR DNASU; 1148628; -.
DR EnsemblBacteria; AAM87229; AAM87229; y3681.
DR EnsemblBacteria; AAS63833; AAS63833; YP_3685.
DR GeneID; 66842944; -.
DR KEGG; ype:YPO0494; -.
DR KEGG; ypk:y3681; -.
DR KEGG; ypm:YP_3685; -.
DR PATRIC; fig|214092.21.peg.744; -.
DR eggNOG; COG0760; Bacteria.
DR HOGENOM; CLU_034646_11_0_6; -.
DR OMA; EGGDMGW; -.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; 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; 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..434
FT /note="Chaperone SurA"
FT /id="PRO_0000270055"
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 434 AA; 47733 MW; 238F66EE627D992E CRC64;
MKNWRTLILG LVICANTAFA APQEVDKVAA VVDNGVVLQS DIDGLLQSVK MNAQQSGQQV
PDDSTLRHQI LERLIMDNIQ LQMAKKMGIT ITDQALDKAI ADIAAQNRMT LAQMRSRLAA
DGLSYDTYRE QIRKEMLTSE VRNNEVRRRI TILPQEVESL AKQMGNQVSG DTELNLSHIL
IPLPENPTQQ QVDQAEDLAN KLVADIKGGA DFGKLAIANS ADSQALKGGQ MGWGKLQELP
SLFAERLQSA HKGEIVGPIR SGVGFHILKV NDMRGADQTI SVTEVNARHI LLKPSPMMTD
EQARAKLEAA AAEIKSGKTS FATIAKEISQ DPGSAMQGGE LGWASPDIYD PAFRDALMKL
KKGEISAPVH SSFGWHLIQL VDTRQVDKTD AAQKERAYRM LFNRKFAEEA QTWMQEQRAA
AYVKILDGSN AQPQ