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Database: UniProt
Entry: A0A1I3RF18_9GAMM
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ID   A0A1I3RF18_9GAMM        Unreviewed;       434 AA.
AC   A0A1I3RF18;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
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=SAMN05421680_109115 {ECO:0000313|EMBL:SFJ45163.1};
OS   Xenorhabdus mauleonii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=351675 {ECO:0000313|EMBL:SFJ45163.1, ECO:0000313|Proteomes:UP000198919};
RN   [1] {ECO:0000313|Proteomes:UP000198919}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17908 {ECO:0000313|Proteomes:UP000198919};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FORG01000009; SFJ45163.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I3RF18; -.
DR   STRING; 351675.SAMN05421680_109115; -.
DR   OrthoDB; 14196at2; -.
DR   Proteomes; UP000198919; 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; 2.
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   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..21
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01183"
FT   CHAIN           22..434
FT                   /note="Chaperone SurA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01183"
FT                   /id="PRO_5011803348"
FT   DOMAIN          172..273
FT                   /note="PpiC"
FT                   /evidence="ECO:0000259|PROSITE:PS50198"
FT   DOMAIN          283..383
FT                   /note="PpiC"
FT                   /evidence="ECO:0000259|PROSITE:PS50198"
SQ   SEQUENCE   434 AA;  48330 MW;  DF0174C4CBC0C7E1 CRC64;
     MKNWRSLILG LMFSVSSVAT AAPQELNKVA AVVNNDVILE SDVRSLLQSV KLNAKHAGQQ
     IPDEATLRHQ ILERLITDDI ILQMAKQMQI TIPDQAVESA ITDIAAQNHM SIAQLKQNLT
     TDGISFDSYR NQIRKEMMIA EVRNNEVRRR ISILPQEVDS LANQISGQSN LDTDLNISHI
     LIPLPENPTQ EQLEKSEATV KKILSELKNG ADFGKLAIAY SGDTQALKGG NMGWSKLQEL
     PSLFAEQLKS AHKGQVIGPI RSGVGFHILK VNDIRGGRAS TSVTEVDARH ILLKTSPVMD
     DELARTELTQ LREEILSGKT TFEKAAKEYS EDPGSAMRGG ELGWNLPTAY DPAFRDALMK
     LEKGEISQPI HSSFGWHLIQ LIDTRKVDKT DAAEKDRAYR LLFNRKFNEE AQNWMQELRA
     SAYVKILDGS NAKQ
//
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