ID A0A1F4JFD5_9BURK Unreviewed; 472 AA.
AC A0A1F4JFD5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=A3I66_23655 {ECO:0000313|EMBL:OGB20727.1};
OS Burkholderiales bacterium RIFCSPLOWO2_02_FULL_57_36.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales.
OX NCBI_TaxID=1797562 {ECO:0000313|EMBL:OGB20727.1, ECO:0000313|Proteomes:UP000176765};
RN [1] {ECO:0000313|EMBL:OGB20727.1, ECO:0000313|Proteomes:UP000176765}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGB20727.1}.
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; MESE01000143; OGB20727.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F4JFD5; -.
DR STRING; 1797562.A3I66_23655; -.
DR Proteomes; UP000176765; 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; PF13616; Rotamase_3; 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 Coiled coil {ECO:0000256|SAM:Coils};
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..30
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01183"
FT CHAIN 31..472
FT /note="Chaperone SurA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01183"
FT /id="PRO_5009730036"
FT DOMAIN 205..305
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
FT DOMAIN 322..421
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
FT COILED 340..367
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 472 AA; 52839 MW; 374CC3CEE9C96A88 CRC64;
MTVFHTMHTV RKPIRSIKLA IILLSAACSA APAAWAQAQG NASRAISPSG APARVQVVAT
IVAVVNNEVI TSQELDGRMR QVESQMKSQG VAMPPRAQLQ KQILERLIVD RAQMQLAKEV
GIRVDDLTLD RAIARIAEQN KMSLQEFRSQ LEREGTPFGR FREEIREEII IQRVREREVA
NKIQITESEV DNYLAANKDA LQNEQQEINL AQILIRIPEN ASAEQIAQRR QKAEEAVQKL
SEGNEFAKVA AAYSDAGDSL KGGELGWRTL ERLPQLFVDA VANVKQGDLA LIKSANGFHI
LKLLGKRTAV PAAKDGTQGL AVQQTHARHI LIKVNQVVSS SEARRKLVEL KERLDNKSAK
FEDLAKLHSN DFSASKGGDL GWIYPGDTVP EFERAMNALQ PGQVSEPVES PFGYHLIQVL
ERKTDDVSKE RQRLVARQML RERKLVEATE DWLRQLRDRA YVEYRLDENS AS
//
