ID A0A2S0MYV3_9BURK Unreviewed; 457 AA.
AC A0A2S0MYV3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=C6571_07035 {ECO:0000313|EMBL:AVO41074.1};
OS Simplicispira suum.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Simplicispira.
OX NCBI_TaxID=2109915 {ECO:0000313|EMBL:AVO41074.1, ECO:0000313|Proteomes:UP000239326};
RN [1] {ECO:0000313|EMBL:AVO41074.1, ECO:0000313|Proteomes:UP000239326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC1-8 {ECO:0000313|EMBL:AVO41074.1,
RC ECO:0000313|Proteomes:UP000239326};
RA Kim S.-J., Heo J., Kwon S.-W.;
RT "Genome sequencing of Simplicispira sp.";
RL Submitted (MAR-2018) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP027669; AVO41074.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S0MYV3; -.
DR KEGG; simp:C6571_07035; -.
DR OrthoDB; 14196at2; -.
DR Proteomes; UP000239326; 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-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; 1.
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|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01183};
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..23
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01183"
FT CHAIN 24..457
FT /note="Chaperone SurA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01183"
FT /id="PRO_5015790276"
FT DOMAIN 199..300
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
FT DOMAIN 311..410
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 457 AA; 49565 MW; F6224F1789317070 CRC64;
MHPRVFAIGL ACLAGALAAP ATAQGVRVPG ARPAPALQPP AARSASAEPQ AADFIVAVVN
SEPITRNELA ARVQRVRKQL ASQNGAMPPE DALAREVLER LIFEKVQLQA AQQAGIGVTD
LAIDQAEASV AQQNDVSRET MYRQLKADGI TPEQFRKELR TQLVLQRLRE REASTHAKVN
EFEIDQYLRD QQPQNGAAGL ELNLGHILIA VPEGASDAVL AEREQRARSV AERARKGADF
SALAKEFSDA PEATQGGQMG LRPADRYPEL FVNASGALAV GGVAGPLRSG AGFHVLKVLE
KRRSDTAAAT VVQSHARHIL LRTGAQLSEA AAAAQLAEYR QRILAGRATF EDLAREHSQD
GSAAQGGNLG WSTPGRYVPE FEAVLEALKP GEISQPVVSR FGVHLIELLE RRQVKLTPRE
QRDVAREALR QKKAEEAYAT WARELRGRAY VEYRDPA
//
