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Database: UniProt
Entry: A0A1M6YUH7_9PROT
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ID   A0A1M6YUH7_9PROT        Unreviewed;       446 AA.
AC   A0A1M6YUH7;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 33.
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=SAMN05216428_101512 {ECO:0000313|EMBL:SHL21689.1};
OS   Nitrosospira sp. Nsp11.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosospira.
OX   NCBI_TaxID=1855338 {ECO:0000313|EMBL:SHL21689.1, ECO:0000313|Proteomes:UP000184455};
RN   [1] {ECO:0000313|Proteomes:UP000184455}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nsp11 {ECO:0000313|Proteomes:UP000184455};
RA   Varghese N., Submissions S.;
RL   Submitted (NOV-2016) 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}.
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DR   EMBL; FRBV01000001; SHL21689.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M6YUH7; -.
DR   STRING; 1855338.SAMN05216428_101512; -.
DR   Proteomes; UP000184455; 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; 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; 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|HAMAP-Rule:MF_01183, ECO:0000256|PROSITE-
KW   ProRule:PRU00278};
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..446
FT                   /note="Chaperone SurA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01183"
FT                   /id="PRO_5013410383"
FT   DOMAIN          181..282
FT                   /note="PpiC"
FT                   /evidence="ECO:0000259|PROSITE:PS50198"
FT   DOMAIN          293..391
FT                   /note="PpiC"
FT                   /evidence="ECO:0000259|PROSITE:PS50198"
SQ   SEQUENCE   446 AA;  49807 MW;  D5B85394D8905DC5 CRC64;
     MGTKFLLRSP VLMALLATGM IVAQQHAHSG SVETIDHIVA VVNENVITRH ELDEVLSATL
     KQLQKQGVQP PPPAILEKQI LDRIIVNRVQ LQLAKETGLT VSDTELDQTL RRIAQENKMS
     LTEFISALEQ DGVSFNRFRD EIRDEIILVR LKEREVSNRV SVSEGEVDNY LETQEISSGN
     NDEYRIAHIL VTIPENATPS QTEARRLRAE AALALLKNGT EFAQVAAEYS DAPDAMTGGL
     LDWRPAAQLT KKFAELLTPM KPGGITPIVS SPGGLHILKL VDRRSPQGAV TVVDQTHVRH
     ILVKISELTS EADARRRVSE LKERLDHGGS FEELAKLHSE DSASSSGGDL GWVSPGDTVP
     EFEQAMNALE PNQVSEPVQS PFGWHLIQVL ARRSQDVSQE RQRQTARQSI RTRKADEAFQ
     DWLQRLRDRA YVEYRLEEGQ DRHAAE
//
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