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Database: UniProt
Entry: A0A0J8GU54_9ALTE
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Original site: A0A0J8GU54_9ALTE 
ID   A0A0J8GU54_9ALTE        Unreviewed;       433 AA.
AC   A0A0J8GU54;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 39.
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   ORFNames=XM47_04580 {ECO:0000313|EMBL:KMT66272.1};
OS   Catenovulum maritimum.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Catenovulum.
OX   NCBI_TaxID=1513271 {ECO:0000313|EMBL:KMT66272.1, ECO:0000313|Proteomes:UP000037600};
RN   [1] {ECO:0000313|EMBL:KMT66272.1, ECO:0000313|Proteomes:UP000037600}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Q1 {ECO:0000313|EMBL:KMT66272.1,
RC   ECO:0000313|Proteomes:UP000037600};
RA   Li Y., Li D., Chen G., Du Z.;
RT   "Draft Genome Sequence of the Novel Agar-Digesting Marine Bacterium Q1.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-
CC         Rule:MF_01183};
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 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:0000256|HAMAP-Rule:MF_01183}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KMT66272.1}.
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DR   EMBL; LAZL01000005; KMT66272.1; -; Genomic_DNA.
DR   RefSeq; WP_048690262.1; NZ_KQ130484.1.
DR   AlphaFoldDB; A0A0J8GU54; -.
DR   STRING; 1513271.XM47_04580; -.
DR   PATRIC; fig|1513271.3.peg.948; -.
DR   OrthoDB; 14196at2; -.
DR   Proteomes; UP000037600; Unassembled WGS sequence.
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   Gene3D; 1.10.4030.10; Porin chaperone SurA, peptide-binding domain; 2.
DR   HAMAP; MF_01183; Chaperone_SurA; 1.
DR   InterPro; IPR046357; PPIase_dom_sf.
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_sf.
DR   PANTHER; PTHR47637; CHAPERONE SURA; 1.
DR   PANTHER; PTHR47637:SF1; CHAPERONE SURA; 1.
DR   Pfam; PF00639; Rotamase; 1.
DR   Pfam; PF13616; Rotamase_3; 1.
DR   Pfam; PF09312; SurA_N; 1.
DR   SUPFAM; SSF54534; FKBP-like; 2.
DR   SUPFAM; SSF109998; Triger factor/SurA peptide-binding domain-like; 1.
DR   PROSITE; PS01096; PPIC_PPIASE_1; 1.
DR   PROSITE; PS50198; PPIC_PPIASE_2; 2.
PE   3: Inferred from homology;
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_01183};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01183, ECO:0000256|PROSITE-
KW   ProRule:PRU00278};
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764, ECO:0000256|HAMAP-Rule:MF_01183};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037600};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_01183};
KW   Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|HAMAP-Rule:MF_01183};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|HAMAP-Rule:MF_01183}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01183"
FT   CHAIN           26..433
FT                   /note="Chaperone SurA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01183"
FT                   /id="PRO_5008990145"
FT   DOMAIN          175..276
FT                   /note="PpiC"
FT                   /evidence="ECO:0000259|PROSITE:PS50198"
FT   DOMAIN          285..385
FT                   /note="PpiC"
FT                   /evidence="ECO:0000259|PROSITE:PS50198"
SQ   SEQUENCE   433 AA;  48052 MW;  32B082998723CFC7 CRC64;
     MKLTKIISLI ILLCANVGTI RSLSAAELLD KVAVVVNQGV ILENEITGMM LQLQAEAKKS
     GQALPSDKAL KVQVTERLIA NELQLQFAER IGLQISDAQV QQQVQQLALQ QNLTLEKFRQ
     NVIASGMDYE TFLERLRQDI TSQEVRQAVV SRRVYVSPQE IDGLVALLKE RGKQTEEYNL
     GHILVGLAPS ASADEIESTQ ERANKIIKLL NSGSDFKKIA IGSSSGAKAL DGGDLGWMNV
     NEMPTLFAEA VVNQKKDDII GPIRSGAGFH ILKITDIRGR QTVEVKEANA RHILIKPTII
     LSDEKAKNML NDFLVKVQAG ELDFSELAKE HSADPGSATK GGELGWADPS MYVPEFKDAL
     ARLNPGEYAQ PFKTVHGWHL VQLIDRRVKD ATENAYQDHA YRMIFNRKFN EEVEAWVREI
     RDQAFVEIVG DAS
//
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