ID A0A099PGB5_9GAMM Unreviewed; 425 AA.
AC A0A099PGB5;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
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};
GN Name=surA {ECO:0000256|HAMAP-Rule:MF_01183};
GN ORFNames=LH51_00135 {ECO:0000313|EMBL:KGK43372.1};
OS Nitrincola sp. A-D6.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Nitrincola.
OX NCBI_TaxID=1545442 {ECO:0000313|EMBL:KGK43372.1, ECO:0000313|Proteomes:UP000029924};
RN [1] {ECO:0000313|EMBL:KGK43372.1, ECO:0000313|Proteomes:UP000029924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A-D6 {ECO:0000313|EMBL:KGK43372.1,
RC ECO:0000313|Proteomes:UP000029924};
RA Valdes N., Rivera-Araya J., Bijman J., Escudero G L., Demergasso C.,
RA Fernandez S., Ferrer A., Chavez R., Levican G.;
RT "Draft Genome Sequence of the Arsenic-Resistant Bacterium Nitrincola sp.
RT Strain A-D6 Isolated from a Salt Flat in Northern Chile.";
RL Submitted (SEP-2014) 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:KGK43372.1}.
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DR EMBL; JRLB01000002; KGK43372.1; -; Genomic_DNA.
DR RefSeq; WP_036518600.1; NZ_JRLB01000002.1.
DR AlphaFoldDB; A0A099PGB5; -.
DR STRING; 1545442.LH51_00135; -.
DR OrthoDB; 14196at2; -.
DR Proteomes; UP000029924; 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; 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; 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|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01183};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764, ECO:0000256|HAMAP-Rule:MF_01183};
KW Reference proteome {ECO:0000313|Proteomes:UP000029924};
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 DOMAIN 169..270
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
FT DOMAIN 279..378
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 425 AA; 47836 MW; 5D760B5E9833D10A CRC64;
MADQSVLTFV LVALFSLHTQ AQQLDRIVAV VNDDIIMKSE LDQRTRLITE QIQGQGVQVP
PADVLRQQVL DRLILDSLQL QIAEIQGLRI SDRQLNETLE AIAAQNGLTL PEFREALIAE
GQDYAQAREQ IRRELLVSQV QQSNVNRRIQ VSEQEIRNFL NSDAAQQRQA EFLLSNILIA
LPSQASPDII QEAERKAEEI YATLTDGAEF ADTAVSVSNA PNALNGGDLG WRNQSELPET
LAAAIANLQP GDISRPIRTP GGFHILQVRD RRGGDVTLVE QTLVSHILLT PNEIRSDEQT
RTLAYDLASR IRDGQPFENL ARRYSDDPGS GSQGGDLGWT QEGQMVPEFE QVMSSTAVDQ
ISEPFESRFG WHVLWVRDRR TQDMSAEMME NMARNTISQR KYNEELDNWL RELRSQAYVE
IRNPG
//
