SURA_XYLFT
ID SURA_XYLFT Reviewed; 463 AA.
AC Q87AJ0;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=PD_1835;
OS Xylella fastidiosa (strain Temecula1 / ATCC 700964).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=183190;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Temecula1 / ATCC 700964;
RX PubMed=12533478; DOI=10.1128/jb.185.3.1018-1026.2003;
RA Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., Miyaki C.Y.,
RA Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H., Takita M.A.,
RA Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R., Goldman M.H.S.,
RA Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M., Carrer H.,
RA Carraro D.M., de Oliveira R.C., Nunes L.R., Siqueira W.J., Coutinho L.L.,
RA Kimura E.T., Ferro E.S., Harakava R., Kuramae E.E., Marino C.L.,
RA Giglioti E., Abreu I.L., Alves L.M.C., do Amaral A.M., Baia G.S.,
RA Blanco S.R., Brito M.S., Cannavan F.S., Celestino A.V., da Cunha A.F.,
RA Fenille R.C., Ferro J.A., Formighieri E.F., Kishi L.T., Leoni S.G.,
RA Oliveira A.R., Rosa V.E. Jr., Sassaki F.T., Sena J.A.D., de Souza A.A.,
RA Truffi D., Tsukumo F., Yanai G.M., Zaros L.G., Civerolo E.L.,
RA Simpson A.J.G., Almeida N.F. Jr., Setubal J.C., Kitajima J.P.;
RT "Comparative analyses of the complete genome sequences of Pierce's disease
RT and citrus variegated chlorosis strains of Xylella fastidiosa.";
RL J. Bacteriol. 185:1018-1026(2003).
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; AE009442; AAO29667.1; -; Genomic_DNA.
DR RefSeq; WP_004088162.1; NC_004556.1.
DR AlphaFoldDB; Q87AJ0; -.
DR SMR; Q87AJ0; -.
DR EnsemblBacteria; AAO29667; AAO29667; PD_1835.
DR GeneID; 58017355; -.
DR KEGG; xft:PD_1835; -.
DR HOGENOM; CLU_034646_11_0_6; -.
DR OMA; EGGDMGW; -.
DR Proteomes; UP000002516; 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; PS50198; PPIC_PPIASE_2; 2.
PE 3: Inferred from homology;
KW Chaperone; Isomerase; Periplasm; Repeat; Rotamase; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01183"
FT CHAIN 26..463
FT /note="Chaperone SurA"
FT /id="PRO_0000270054"
FT DOMAIN 175..277
FT /note="PpiC 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01183"
FT DOMAIN 291..390
FT /note="PpiC 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01183"
FT REGION 439..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 463 AA; 50730 MW; 8F0CFFE47C6429C7 CRC64;
MTRYFSIVLS LLLAVSCVFL PVASARQQQH QPLDRIVAVV DDNVVLKSEL DRAIHNVKSQ
YVGHEGQLPP DEVLQRQVLE RLILIKLQVA RAQTNGIRVS DDELNQAISS IAENNKTSVD
GLRQKLVAEG ISFPEFRQSV RDEITVHHLR QGFAQSRIVV SEGEVDTALA QANSGAQYHL
QHILVSLPDG ATSEQIAIAQ KKINGIKSVI DKGELAFSAA AVRYSDSPNA LESGDLGWRS
LDEIPEAFAQ MVQTMKPGQI VGPLRGTSGF QLLKLVEVRD STAAAGPRQM ATEYHARHIL
VRITDKQKEA QAKAKIDTLR ARIAGGADFQ TVARESSEDA NNSNQGGDLG WFPSDAFGAD
FGNHVKALAD GNVSEPFRSA AGWHIVQRLG TRQTDVTREN QRAQIRDTIG QRKLEESYER
FLRELRSEAY VSLQIEEPAD DHHTPSAAVT PATGAVLPAA TKH
