ID SURA_BORPE Reviewed; 519 AA.
AC Q7VU12;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=Chaperone SurA {ECO:0000255|HAMAP-Rule:MF_01183};
DE AltName: Full=Peptidyl-prolyl cis-trans isomerase SurA {ECO:0000255|HAMAP-Rule:MF_01183};
DE Short=PPIase SurA {ECO:0000255|HAMAP-Rule:MF_01183};
DE EC=5.2.1.8 {ECO:0000255|HAMAP-Rule:MF_01183};
DE AltName: Full=Rotamase SurA {ECO:0000255|HAMAP-Rule:MF_01183};
DE Flags: Precursor;
GN Name=surA {ECO:0000255|HAMAP-Rule:MF_01183}; OrderedLocusNames=BP3330;
OS Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257313;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(2003).
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:0000255|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:0000255|HAMAP-
CC Rule:MF_01183};
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_01183}.
CC Note=Is capable of associating with the outer membrane.
CC {ECO:0000255|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:0000255|HAMAP-Rule:MF_01183}.
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DR EMBL; BX640421; CAE43595.1; -; Genomic_DNA.
DR RefSeq; NP_881866.1; NC_002929.2.
DR RefSeq; WP_010931412.1; NZ_CP039022.1.
DR AlphaFoldDB; Q7VU12; -.
DR SMR; Q7VU12; -.
DR STRING; 257313.BP3330; -.
DR PaxDb; 257313-BP3330; -.
DR GeneID; 69600667; -.
DR KEGG; bpe:BP3330; -.
DR PATRIC; fig|257313.5.peg.3609; -.
DR eggNOG; COG0760; Bacteria.
DR HOGENOM; CLU_034646_11_0_4; -.
DR Proteomes; UP000002676; Chromosome.
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; Isomerase; Periplasm; Reference proteome; Repeat; Rotamase;
KW Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01183"
FT CHAIN 32..519
FT /note="Chaperone SurA"
FT /id="PRO_0000270004"
FT DOMAIN 223..324
FT /note="PpiC 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01183"
FT DOMAIN 364..463
FT /note="PpiC 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01183"
FT REGION 31..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 519 AA; 56858 MW; 9AC7B5A2ADB5417D CRC64;
MMRSLHSLRR MSGTVLALML AAGLPLSAAQ AQPAKPAPKG DQKPATPAPS EQFVDGIAAI
VNKDVITLRE VREASKLASA DLQKRGIQVP DERTLQKQVL QRLIMERLER QEADRMGIRV
DEAQVDQAIN MIASRNKITP AAMRAEIEKS GVTWEQYRKS LRDDIRMDRL RQRAVDANII
ISDAEVDAFL KDQERNPAAA QATRAPAPQQ PQPQPRQPAQ SGPAMLVLAQ ILVRVPEGSS
PDQVAALRKK AEGLLARAKK GDDFASLAAA NSDGPEALQG GMMGARPLDG WPDLFVKAAG
SLSAGQVSGL VQSGNGFHIL KVVDRAGGGQ PAQAARPAPA PAPQQPSSFQ EGPSVAAPQG
PVRVTQTHAR HILIKTSTVM TDDQARQRLE QIRERLQGGA VKFEDMARQY SQDSTAPQGG
DLGWVNPGDT VPPFEAAMNA LQPNEISPPM LSPFGWHLIQ VLERREHDVS DEVQRMRARQ
LLFERRAVPA FEDWLEQLRS QAFIDNRLEK QERLEQNNR
//
