ID   SURA_METCA              Reviewed;         454 AA.
AC   Q60B78;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=MCA0602;
OS   Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales;
OC   Methylococcaceae; Methylococcus.
OX   NCBI_TaxID=243233;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33009 / NCIMB 11132 / Bath;
RX   PubMed=15383840; DOI=10.1371/journal.pbio.0020303;
RA   Ward N.L., Larsen O., Sakwa J., Bruseth L., Khouri H.M., Durkin A.S.,
RA   Dimitrov G., Jiang L., Scanlan D., Kang K.H., Lewis M.R., Nelson K.E.,
RA   Methe B.A., Wu M., Heidelberg J.F., Paulsen I.T., Fouts D.E., Ravel J.,
RA   Tettelin H., Ren Q., Read T.D., DeBoy R.T., Seshadri R., Salzberg S.L.,
RA   Jensen H.B., Birkeland N.K., Nelson W.C., Dodson R.J., Grindhaug S.H.,
RA   Holt I.E., Eidhammer I., Jonasen I., Vanaken S., Utterback T.R.,
RA   Feldblyum T.V., Fraser C.M., Lillehaug J.R., Eisen J.A.;
RT   "Genomic insights into methanotrophy: the complete genome sequence of
RT   Methylococcus capsulatus (Bath).";
RL   PLoS Biol. 2:1616-1628(2004).
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; AE017282; AAU93127.1; -; Genomic_DNA.
DR   RefSeq; WP_010959947.1; NC_002977.6.
DR   AlphaFoldDB; Q60B78; -.
DR   SMR; Q60B78; -.
DR   STRING; 243233.MCA0602; -.
DR   PRIDE; Q60B78; -.
DR   EnsemblBacteria; AAU93127; AAU93127; MCA0602.
DR   KEGG; mca:MCA0602; -.
DR   eggNOG; COG0760; Bacteria.
DR   HOGENOM; CLU_034646_11_0_6; -.
DR   OMA; EGGDMGW; -.
DR   OrthoDB; 1838755at2; -.
DR   Proteomes; UP000006821; 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   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   Pfam; PF00639; Rotamase; 1.
DR   Pfam; PF09312; SurA_N; 1.
DR   SUPFAM; SSF109998; SSF109998; 1.
DR   PROSITE; PS01096; PPIC_PPIASE_1; 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..28
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01183"
FT   CHAIN           29..454
FT                   /note="Chaperone SurA"
FT                   /id="PRO_0000270021"
FT   DOMAIN          177..278
FT                   /note="PpiC 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01183"
FT   DOMAIN          287..386
FT                   /note="PpiC 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01183"
FT   REGION          431..454
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   454 AA;  50789 MW;  C5FE34F1B0886AEA CRC64;
     MKISSFRKGR WLGALALFAV VCWSMADAAV DRIVAVVDDG VILESELVRK VDEIKRSLRA
     SRASLPPDSV LVRQVLERMI VDKIQIQMAE KMGIQVDDDT LRMAVSQIAQ RNNLTPDQFR
     RSLAREGIDY GDFLDQVRSE IAMGRLRASQ INNQIKISDR EVEHYLEAQG GSGAVADREY
     RLGHILIATP REASPDEVKK ARERADRVVK ELKAGLDFKD ASIRYSDDPQ ALEGGDLGWR
     KLSEIPSHIA EVVGGMKDGE VSDPIRSPGG YHIVKMLAMR GVGEAKLTKT HVRHILIRPN
     EVLSDEDAKN KLLALKTRIE NGDDFAELAR GHSDDKGSAI KGGDLGWVKP GALVPPFEEA
     MNALDENQLS DPVQTQFGWH LIQVLERQES SDTNEVLKNR ARDELFKRKV DEETELWLRK
     IRDEAYVEIR LDETPASPGE DAPAGEDSPE TFMR