ID A0A2X2E2X1_RAOPL Unreviewed; 428 AA.
AC A0A2X2E2X1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 32.
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 ECO:0000313|EMBL:SBM05204.1};
GN ORFNames=DN603_00890 {ECO:0000313|EMBL:RWT26143.1}, SAMEA2273876_02365
GN {ECO:0000313|EMBL:SBM05204.1};
OS Raoultella planticola (Klebsiella planticola).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Raoultella.
OX NCBI_TaxID=575 {ECO:0000313|EMBL:RWT26143.1, ECO:0000313|Proteomes:UP000288843};
RN [1] {ECO:0000313|EMBL:SBM05204.1, ECO:0000313|Proteomes:UP000078124}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2880STDY5682802 {ECO:0000313|EMBL:SBM05204.1,
RC ECO:0000313|Proteomes:UP000078124};
RG Pathogen Informatics;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RWT26143.1, ECO:0000313|Proteomes:UP000288843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GEO_47_Down_B {ECO:0000313|EMBL:RWT26143.1,
RC ECO:0000313|Proteomes:UP000288843};
RA Mathys D.A., Mollenkopf D.F., Feicht S.M., Adams R.J., Albers A.L.,
RA Stuever D.M., Daniels J.B., Wittum T.E.;
RT "Carbapenemase-producing Enterobacteriaceae present in wastewater treatment
RT plant effluent and nearby surface waters in the US.";
RL Submitted (JUN-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 -!- 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:RWT26143.1}.
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DR EMBL; QKOX01000001; RWT26143.1; -; Genomic_DNA.
DR EMBL; FLAC01000008; SBM05204.1; -; Genomic_DNA.
DR RefSeq; WP_032689512.1; NZ_VNVX01000002.1.
DR AlphaFoldDB; A0A2X2E2X1; -.
DR GeneID; 72407205; -.
DR KEGG; rpln:B1209_22920; -.
DR Proteomes; UP000078124; Unassembled WGS sequence.
DR Proteomes; UP000288843; 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|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..20
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01183"
FT CHAIN 21..428
FT /note="Chaperone SurA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01183"
FT /id="PRO_5034921179"
FT DOMAIN 171..272
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
FT DOMAIN 282..382
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 428 AA; 47179 MW; 4601C7FE7435F3B9 CRC64;
MKNWKTLLLG IAMIANTSFA APQVVDKVAA VVNNGVVLES DVDGLLQSVK LNAGQAGQQL
PDDATLRHQI LERLIMDQIV LQMGQKMGMK ITDDQVDQAI ANIAKQNNMT MDQMRSRLAY
DGLNYNTYRN QIRKEMLIAE VRNNEVRRRI TVLPQEVESL AKQIGDQNDA STELNLSHIL
IPLTENPTSD DVAKAQEQAN AIVEQARSGA DFGKLAITYS ADQQALKGGQ MGWGRIQELP
GIFAQALSTA KKGDIVGPIR SGVGFHILKV NDMRGGSKNI SVTEVHARHI LLKPSPIMND
DQARAKLEQI AADIKSGKTT FAKAAKEFSE DPGSANQGGD LGWATPDIFD PAFRDALMRL
NKGQTSAPVH SSFGWHLIQL MDSRQVDRTD AAQKDRAYRM LMNRKFSEEA ATWMQEQRAS
AYVKILSN
//
