(data stored in ACNUC7421 zone)

SWISSPROT: C5B7P3_EDWI9

ID   C5B7P3_EDWI9            Unreviewed;       434 AA.
AC   C5B7P3;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 62.
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   OrderedLocusNames=NT01EI_0698 {ECO:0000313|EMBL:ACR67920.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67920.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001600; ACR67920.1; -; Genomic_DNA.
DR   RefSeq; WP_015870113.1; NC_012779.2.
DR   ProteinModelPortal; C5B7P3; -.
DR   STRING; 634503.NT01EI_0698; -.
DR   EnsemblBacteria; ACR67920; ACR67920; NT01EI_0698.
DR   GeneID; 7962032; -.
DR   KEGG; eic:NT01EI_0698; -.
DR   PATRIC; fig|634503.3.peg.629; -.
DR   eggNOG; ENOG4105DBD; Bacteria.
DR   eggNOG; COG0760; LUCA.
DR   HOGENOM; HOG000264337; -.
DR   KO; K03771; -.
DR   OMA; EMIISRV; -.
DR   OrthoDB; POG091H06DX; -.
DR   Proteomes; UP000001485; 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; IPR023058; PPIase_PpiC_CS.
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; PS01096; PPIC_PPIASE_1; 1.
DR   PROSITE; PS50198; PPIC_PPIASE_2; 2.
PE   3: Inferred from homology;
DR   PRODOM; C5B7P3.
DR   SWISS-2DPAGE; C5B7P3.
KW   Chaperone {ECO:0000256|HAMAP-Rule:MF_01183,
KW   ECO:0000256|SAAS:SAAS00502901};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01183, ECO:0000256|PROSITE-
KW   ProRule:PRU00278, ECO:0000256|SAAS:SAAS00523002};
KW   Periplasm {ECO:0000256|HAMAP-Rule:MF_01183};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485};
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     20       {ECO:0000256|HAMAP-Rule:MF_01183}.
FT   CHAIN        21    434       Chaperone SurA. {ECO:0000256|HAMAP-Rule:
FT                                MF_01183}.
FT                                /FTId=PRO_5009008510.
FT   DOMAIN      171    272       PpiC. {ECO:0000259|PROSITE:PS50198}.
FT   DOMAIN      282    382       PpiC. {ECO:0000259|PROSITE:PS50198}.
SQ   SEQUENCE   434 AA;  47857 MW;  7E74E21894B25731 CRC64;
     MKNWRTLILG VALCANTAFA APQVVDKVVA IVDNGVVLES DVDGMMKSVK LNAQQAGQQL
     PDDATLRHQI LERLIMDNVQ LQMAKRMGLE ISDSELDNAI NGIAQQNHIS MQQLRSRLAA
     DGLDYKTYRD QIRKEMLISE VRNNEVRSRV TILPQEVDAL AKQIGSQNSG ETAVNLSHIL
     IPLPENPTQQ QVSEAQKQAE SLIQQLHQGA SFAKLAAAYS ADPQALKGGE MGWGRLQELP
     TLFAEALQSA KKGDIVGPIR SGVGFHILRV NDLRGDQASV SVTEVHARHI LLRPSPVMSD
     TQARAKLEAL SAQIKSGQIT FEQAAKEYSQ DPGSAQKGGD LGWAVPSMYD PAFRDALMKL
     NKGEISQPVH SNFGWHLIQL LDTRQVDRTD EAQKERAYRM LFNRKFAEEA QTWLQEQRAA
     AYVKILGNSA NGAQ
//

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