ID A0A7Y4P6E0_9BURK Unreviewed; 493 AA.
AC A0A7Y4P6E0;
DT 02-JUN-2021, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 1.
DT 02-APR-2025, entry version 16.
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=HKX40_06735 {ECO:0000313|EMBL:NOL49829.1};
OS Pelistega europaea.
OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC Burkholderiales; Alcaligenaceae; Pelistega.
OX NCBI_TaxID=106147 {ECO:0000313|EMBL:NOL49829.1, ECO:0000313|Proteomes:UP000541421};
RN [1] {ECO:0000313|EMBL:NOL49829.1, ECO:0000313|Proteomes:UP000541421}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG10982 {ECO:0000313|EMBL:NOL49829.1,
RC ECO:0000313|Proteomes:UP000541421};
RA Niu N.;
RL Submitted (MAY-2020) 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:NOL49829.1}.
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DR EMBL; JABGBO010000006; NOL49829.1; -; Genomic_DNA.
DR RefSeq; WP_171588803.1; NZ_JABGBO010000006.1.
DR AlphaFoldDB; A0A7Y4P6E0; -.
DR Proteomes; UP000541421; 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; IPR050280; OMP_Chaperone_SurA.
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:UP000541421};
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..27
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01183"
FT CHAIN 28..493
FT /note="Chaperone SurA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01183"
FT /id="PRO_5031656836"
FT DOMAIN 203..304
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
FT DOMAIN 343..441
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 493 AA; 55178 MW; 32F90A1B6B0A96E0 CRC64;
MQYSKTWLKI ALIALPGLVL TAPEALAAKA THKVTKQRQG TFADGIAAVV NTDIITMKQL
DSRMRAMEVS GNPVSKEEAL SLLIDEHLMN SQAEQLGIRV TQERLRDVLN GIAQENGMTL
EQLQQAAKQH GINWDDYVAN MAEQVRMEDL RSQVVQSRVH VSEFDVKAFL AQHPTGMYPE
YKKNVVSQPR YEKREVIERS FDPKAVAFQH IYIRVPEGAS DEEVAAAKKK ADEALAKIRR
GASFASVARQ YSDGAEAKNG GDLGIRMNED WPELFMAVTK KVRDGGTTGV FKASNGFHIL
RVVERRGIVN EQRKVVNVRL PDPPQAQLTP REQAARHDGP VEVTDTHVRH ILIRVTPVFS
DAQAKAKIDD IYQKLQSGQQ FADLAEKYSQ DSSAPLGGDI GWVTPGQSDP AFEQAMASLQ
PGQVSAPVRS KFGWHILEVL DRRTEDKQAS IRHDLAYETL YQEQAQHVLQ DWLSQLRSQA
YIDNRLTGQT NRK
//
