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-MAY-2013, entry version 44.
DE RecName: Full=Chaperone SurA;
DE AltName: Full=Peptidyl-prolyl cis-trans isomerase SurA;
DE Short=PPIase SurA;
DE EC=5.2.1.8;
DE AltName: Full=Rotamase SurA;
DE Flags: Precursor;
GN Name=surA; 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 (By similarity).
CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC (omega=0).
CC -!- SUBCELLULAR LOCATION: Periplasm (By similarity). Note=Is capable
CC of associating with the outer membrane (By similarity).
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 (By similarity).
CC -!- SIMILARITY: Contains 2 PpiC domains.
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DR EMBL; CP000083; AAZ28113.1; -; Genomic_DNA.
DR RefSeq; YP_271172.1; NC_003910.7.
DR HSSP; P24327; 1ZK6.
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; FGVHLIQ; -.
DR BioCyc; CPSY167879:GI48-4533-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: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:0000413; P:protein peptidyl-prolyl isomerization; IEA:GOC.
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; Trigger_fac_C_bac; 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; Repeat; Rotamase;
KW Signal.
FT SIGNAL 1 24 Potential.
FT CHAIN 25 433 Chaperone SurA.
FT /FTId=PRO_0000270012.
FT DOMAIN 175 276 PpiC 1.
FT DOMAIN 285 384 PpiC 2.
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
//
