(data stored in ACNUC7421 zone)

SWISSPROT: A0A0H2ZLB3_PSEAB

ID   A0A0H2ZLB3_PSEAB        Unreviewed;       430 AA.
AC   A0A0H2ZLB3;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   07-JUN-2017, entry version 15.
DE   RecName: Full=Chaperone SurA {ECO:0000256|HAMAP-Rule:MF_01183};
DE   AltName: Full=Peptidyl-prolyl cis-trans isomerase SurA {ECO:0000256|HAMAP-Rule:MF_01183};
DE            Short=PPIase SurA {ECO:0000256|HAMAP-Rule:MF_01183};
DE            EC=5.2.1.8 {ECO:0000256|HAMAP-Rule:MF_01183};
DE   AltName: Full=Rotamase SurA {ECO:0000256|HAMAP-Rule:MF_01183};
DE   Flags: Precursor;
GN   Name=surA {ECO:0000256|HAMAP-Rule:MF_01183,
GN   ECO:0000313|EMBL:ABJ15558.1};
GN   OrderedLocusNames=PA14_07760 {ECO:0000313|EMBL:ABJ15558.1};
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963 {ECO:0000313|EMBL:ABJ15558.1, ECO:0000313|Proteomes:UP000000653};
RN   [1] {ECO:0000313|EMBL:ABJ15558.1, ECO:0000313|Proteomes:UP000000653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14 {ECO:0000313|EMBL:ABJ15558.1,
RC   ECO:0000313|Proteomes:UP000000653};
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
CC   -!- FUNCTION: Chaperone involved in the correct folding and assembly
CC       of outer membrane proteins. Recognizes specific patterns of
CC       aromatic residues and the orientation of their side chains, which
CC       are found more frequently in integral outer membrane proteins. May
CC       act in both early periplasmic and late outer membrane-associated
CC       steps of protein maturation. {ECO:0000256|HAMAP-Rule:MF_01183}.
CC   -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC       (omega=0). {ECO:0000256|HAMAP-Rule:MF_01183,
CC       ECO:0000256|SAAS:SAAS00523013}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|HAMAP-Rule:MF_01183}.
CC       Note=Is capable of associating with the outer membrane.
CC       {ECO:0000256|HAMAP-Rule:MF_01183}.
CC   -!- DOMAIN: The PPIase activity resides only in the second parvulin
CC       domain. The N-terminal region and the C-terminal tail are
CC       necessary and sufficient for the chaperone activity of SurA. The
CC       PPIase activity is dispensable for SurA to function as a
CC       chaperone. The N-terminal region and the C-terminal tail are also
CC       required for porin recognition. {ECO:0000256|HAMAP-Rule:MF_01183}.
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DR   EMBL; CP000438; ABJ15558.1; -; Genomic_DNA.
DR   RefSeq; WP_003109024.1; NC_008463.1.
DR   ProteinModelPortal; A0A0H2ZLB3; -.
DR   EnsemblBacteria; ABJ15558; ABJ15558; PA14_07760.
DR   KEGG; pau:PA14_07760; -.
DR   KO; K03771; -.
DR   OMA; EMIISRV; -.
DR   Proteomes; UP000000653; 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-HAMAP.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0051085; P:chaperone mediated protein folding requiring cofactor; IEA:InterPro.
DR   GO; GO:0043165; P:Gram-negative-bacterium-type cell outer membrane assembly; IEA:InterPro.
DR   GO; GO:0060274; P:maintenance of stationary phase; IEA:InterPro.
DR   GO; GO:0050821; P:protein stabilization; IEA:InterPro.
DR   HAMAP; MF_01183; Chaperone_SurA; 1.
DR   InterPro; IPR000297; PPIase_PpiC.
DR   InterPro; IPR023034; PPIase_SurA.
DR   InterPro; IPR015391; SurA_N.
DR   InterPro; IPR027304; Trigger_fact/SurA_dom.
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;
DR   PRODOM; A0A0H2ZLB3.
DR   SWISS-2DPAGE; A0A0H2ZLB3.
KW   Chaperone {ECO:0000256|HAMAP-Rule:MF_01183,
KW   ECO:0000256|SAAS:SAAS00502901};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000653};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01183, ECO:0000256|PROSITE-
KW   ProRule:PRU00278, ECO:0000256|SAAS:SAAS00523002,
KW   ECO:0000313|EMBL:ABJ15558.1};
KW   Periplasm {ECO:0000256|HAMAP-Rule:MF_01183};
KW   Repeat {ECO:0000256|HAMAP-Rule:MF_01183,
KW   ECO:0000256|SAAS:SAAS00015058};
KW   Rotamase {ECO:0000256|HAMAP-Rule:MF_01183, ECO:0000256|PROSITE-
KW   ProRule:PRU00278, ECO:0000256|SAAS:SAAS00522988};
KW   Signal {ECO:0000256|HAMAP-Rule:MF_01183}.
FT   SIGNAL        1     25       {ECO:0000256|HAMAP-Rule:MF_01183}.
FT   CHAIN        26    430       Chaperone SurA. {ECO:0000256|HAMAP-Rule:
FT                                MF_01183}.
FT                                /FTId=PRO_5008988693.
FT   DOMAIN      176    277       PpiC. {ECO:0000259|PROSITE:PS50198}.
FT   DOMAIN      286    385       PpiC. {ECO:0000259|PROSITE:PS50198}.
SQ   SEQUENCE   430 AA;  48443 MW;  6B357AA04FA962CA CRC64;
     MKIKLCNRLR PLALGAALLC SFAHAEVVPL DRVVAIVDND VIMQSQLDQR LREVHQTLLK
     RGAPLPPEHV LTQQVLERLI IENIQQQIGD RSGIRISDEE LNQAMGTIAQ RNGMSLEQFQ
     AALTRDGLSY ADAREQVRRE MVISRVRQRR VAERIQVSEQ EVKNFLASDM GKIQLSEEYR
     LANILIPVPE AASSDVIQAA ARQAQELYQQ LKQGADFGQL AISRSAGDNA LEGGEIGWRK
     AAQLPQPFDS MIGSLAVGDV TEPVRTPGGF IILKLEEKRG GSKMVRDEVH VRHILLKPSE
     IRSEAETEKL AQKLYERIQS GEDFGELAKS FSEDPGSALN GGDLNWIDPE ALVPEFRQVM
     NDTPQGELSK PFRSQFGWHI LQVLGRRATD SSEKFREQQA VSVLRNRKYD EELQAWLRQI
     RDEAYVEIKQ
//

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