SURA_PSEAE
ID SURA_PSEAE Reviewed; 417 AA.
AC Q9I5U3;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 102.
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=PA0594;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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=AAG03983.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE004091; AAG03983.1; ALT_INIT; Genomic_DNA.
DR PIR; B83572; B83572.
DR RefSeq; NP_249285.1; NC_002516.2.
DR AlphaFoldDB; Q9I5U3; -.
DR SMR; Q9I5U3; -.
DR STRING; 287.DR97_3563; -.
DR PaxDb; Q9I5U3; -.
DR PRIDE; Q9I5U3; -.
DR EnsemblBacteria; AAG03983; AAG03983; PA0594.
DR GeneID; 879552; -.
DR KEGG; pae:PA0594; -.
DR PATRIC; fig|208964.12.peg.630; -.
DR PseudoCAP; PA0594; -.
DR HOGENOM; CLU_034646_11_0_6; -.
DR InParanoid; Q9I5U3; -.
DR OMA; EGGDMGW; -.
DR PhylomeDB; Q9I5U3; -.
DR Proteomes; UP000002438; 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..12
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01183"
FT CHAIN 13..417
FT /note="Chaperone SurA"
FT /id="PRO_0000270026"
FT DOMAIN 163..264
FT /note="PpiC 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01183"
FT DOMAIN 273..372
FT /note="PpiC 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01183"
SQ SEQUENCE 417 AA; 46953 MW; 29720C59D6F63D34 CRC64;
MGAALLCSFA HAEVVPLDRV VAIVDNDVIM QSQLDQRLRE VHQTLLKRGA PLPPEHVLTQ
QVLERLIIEN IQQQIGDRSG IRISDEELNQ AMGTIAQRNG MSLEQFQTAL TRDGLSYADA
REQVRREMVI SRVRQRRVAE RIQVSEQEVK NFLASDMGKI QLSEEYRLAN ILIPVPEAAS
SDVIQAAARQ AQELYQQLKQ GADFGQLAIS RSAGDNALEG GEIGWRKAAQ LPQPFDSMIG
SLAVGDVTEP VRTPGGFIIL KLEEKRGGSK MVRDEVHVRH ILLKPSEIRS EAETEKLAQK
LYERIQSGED FGELAKSFSE DPGSALNGGD LNWIDPEALV PEFRQVMNDT PQGELSKPFR
SQFGWHILQV LGRRATDSSE KFREQQAVSV LRNRKYDEEL QAWLRQIRDE AYVEIKQ
