ID M4U523_9GAMM Unreviewed; 456 AA.
AC M4U523;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 59.
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};
GN Name=surA {ECO:0000256|HAMAP-Rule:MF_01183};
GN ORFNames=PCNPT3_03870 {ECO:0000313|EMBL:AGH80716.1};
OS Psychromonas sp. CNPT3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Psychromonadaceae; Psychromonas.
OX NCBI_TaxID=314282 {ECO:0000313|EMBL:AGH80716.1, ECO:0000313|Proteomes:UP000010320};
RN [1] {ECO:0000313|EMBL:AGH80716.1, ECO:0000313|Proteomes:UP000010320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNPT3 {ECO:0000313|EMBL:AGH80716.1,
RC ECO:0000313|Proteomes:UP000010320};
RA Lauro F.M., Chastain R.A., Stratton T.K., Ferriera S., Johnson J.,
RA Yayanos A.A., Bartlett D.H.;
RT "The complete genome sequence of the deep-sea bacterium Psychromonas
RT CNPT2.";
RL Submitted (MAR-2013) 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; CP004404; AGH80716.1; -; Genomic_DNA.
DR AlphaFoldDB; M4U523; -.
DR STRING; 314282.PCNPT3_03870; -.
DR KEGG; psy:PCNPT3_03870; -.
DR eggNOG; COG0760; Bacteria.
DR HOGENOM; CLU_034646_11_0_6; -.
DR Proteomes; UP000010320; 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; 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:UP000010320};
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 DOMAIN 194..293
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
FT DOMAIN 302..402
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 456 AA; 52202 MW; C9162E31D8D97205 CRC64;
MEMKVYLIMA ALFTYNNGYK MRSIQSLIVT MICTILLSGT VVASTEHLDQ IEAIVNQEVI
LSSDVKRMEK DIRARYLKMQ QALPSKQKLR QQILDKLIND SLQLQVAERM GLRLDNAQVD
QTIQQILKKE GKNIAQYQQE LSRKGQSYQA FSDSVRNELT INEIRQMQVR QRLNISEQEI
NLMVQRLNKD GKKNTQFHFI HILLKTDPNA PLHAQQQAKK IMQRLAQGES ASSLARQYSQ
GPKALDGGDW GWRTVDEIPS LFADKFDELK TKKGDILGPF KTRLGLSIIQ VSDKKGIKNT
TTLEVNARHI LIKSNIILSD KKAKLLLNTY RQEILEGKAN FAELARAHSQ DPGSAVKGGN
LGWADPNMYV PEFRDRAQSL RIGEISKPFH TMHGWHILEV LEKRQADTTE KASKQKAYSI
LYKQRFPAEV YAWMNEIRQE AYIKIVNDKP NAAQKK
//
