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Database: UniProt
Entry: Q47VK0
LinkDB: Q47VK0
Original site: Q47VK0 
ID   SURA_COLP3              Reviewed;         433 AA.
AC   Q47VK0;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   01-OCT-2014, entry version 52.
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};
GN   OrderedLocusNames=CPS_4524;
OS   Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS   psychroerythus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=167879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=34H / ATCC BAA-681;
RX   PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA   Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA   Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA   Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA   Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA   Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT   "The psychrophilic lifestyle as revealed by the genome sequence of
RT   Colwellia psychrerythraea 34H through genomic and proteomic
RT   analyses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005).
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:0000255|HAMAP-Rule:MF_01183}.
CC   -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC       (omega=0). {ECO:0000255|HAMAP-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
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:0000255|HAMAP-Rule:MF_01183}.
CC   -!- SIMILARITY: Contains 2 PpiC domains. {ECO:0000255|HAMAP-
CC       Rule:MF_01183}.
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DR   EMBL; CP000083; AAZ28113.1; -; Genomic_DNA.
DR   RefSeq; WP_011045253.1; NC_003910.7.
DR   RefSeq; YP_271172.1; NC_003910.7.
DR   ProteinModelPortal; Q47VK0; -.
DR   STRING; 167879.CPS_4524; -.
DR   EnsemblBacteria; AAZ28113; AAZ28113; CPS_4524.
DR   GeneID; 3522372; -.
DR   KEGG; cps:CPS_4524; -.
DR   PATRIC; 21471873; VBIColPsy94388_4117.
DR   eggNOG; COG0760; -.
DR   HOGENOM; HOG000264337; -.
DR   KO; K03771; -.
DR   OMA; HERMDEW; -.
DR   OrthoDB; EOG6M9DS4; -.
DR   BioCyc; CPSY167879:GI48-4525-MONOMER; -.
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:0042710; P:biofilm formation; IEA:InterPro.
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;
KW   Chaperone; Complete proteome; Isomerase; Periplasm;
KW   Reference proteome; Repeat; Rotamase; Signal.
FT   SIGNAL        1     24       {ECO:0000255|HAMAP-Rule:MF_01183}.
FT   CHAIN        25    433       Chaperone SurA.
FT                                /FTId=PRO_0000270012.
FT   DOMAIN      175    276       PpiC 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01183}.
FT   DOMAIN      285    384       PpiC 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01183}.
SQ   SEQUENCE   433 AA;  48639 MW;  902AEF5E57D48AF6 CRC64;
     MKYRIKALLL ASSLIITTIT SVQAKEELLD RVAAIVNTGV VLESEVNDLL VNIKQQAKKN
     NQSLPSDKAL RIQVMDKLIN DSLLSQMGQR MGIQISDAQL DQTLNNMARE DKLTLAQFRQ
     QVIDEGTSYE KYRENVRIEL VSGEVSRNSV RRRIFVSPQE VDNLLKVMKE QSSNNVEYHL
     GHILIEFPAD ASQEDLAAAK TRATKVVELL NDGSDFAKIA ITSSGDANAL KGGDLGWKNI
     NEMPTLFSEL INDKPKDTIV GPIRTGLGYS IVKVLDIRGR KVVEVEEVKA SHILIKPSII
     LSDEKAKSLL QGFLNQIDAG EATFEELAKE HSEGPTSVRG GDLGWADPKN YDPAFTEALA
     TMKKGGYHKP FRSSFGWHII KLEDRRMVDA TSQLNENRAY QILFNRKYGM ESTRWLKETR
     DEAYIEIFEQ DNK
//
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