SURA_BURCA
ID SURA_BURCA Reviewed; 452 AA.
AC Q1BTQ6;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=Bcen_2098;
OS Burkholderia cenocepacia (strain AU 1054).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=331271;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU 1054;
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 Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Lykidis A., LiPuma J.J., Konstantinidis K.,
RA Tiedje J.M., Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia cenocepacia AU 1054.";
RL Submitted (MAY-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}.
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DR EMBL; CP000378; ABF76999.1; -; Genomic_DNA.
DR RefSeq; WP_011546172.1; NC_008060.1.
DR AlphaFoldDB; Q1BTQ6; -.
DR SMR; Q1BTQ6; -.
DR EnsemblBacteria; ABF76999; ABF76999; Bcen_2098.
DR KEGG; bcn:Bcen_2098; -.
DR HOGENOM; CLU_034646_11_0_4; -.
DR OMA; EGGDMGW; -.
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; 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; Repeat; Rotamase; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01183"
FT CHAIN 29..452
FT /note="Chaperone SurA"
FT /id="PRO_5000123057"
FT DOMAIN 186..288
FT /note="PpiC 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01183"
FT DOMAIN 302..400
FT /note="PpiC 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01183"
SQ SEQUENCE 452 AA; 49136 MW; 288EDF3E34514292 CRC64;
MKKTLRFAAV VSSLAASAAL LVAAPAAAQA LGSQGAQLAD EVVAVVNNDV ITGRELDQRV
GLIARRLQQQ NAPVPPADQL RAQVLNQMVL ERIQVQKAKD DGIRIDDATV QATLQRLAQA
NGMTLDQYRG RLEAQGVPWS IFTNDARTEL MLSKLREREV DGKITVSDAE VANYIASQRG
PNASQQQDLR FQHIFIKAPT NAPQADIEAA QKKADALLQQ AKSGADFERL AKNNSEANDA
KKGGDLGFKS PSALPADVVD AASKLRPGQV NPTLIRVPDG FEIVRLVDRR QSQGASAAAP
KIVQTHVRHI LLRVGEGKSE GQARQQLVDI RNQVEAGGDF AKFARTYSQD GSASQGGDLG
WISPGETVPE FERAMNNLQD GQISQPIRTE YGYHLIQVLN RREAEGSVQQ QMDIARQAIG
QRKAEQAYAD WLRELRDSSY VQYKIGGVGP AN