ID A0A1C2IN07_ACITH Unreviewed; 479 AA.
AC A0A1C2IN07;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=A6M23_08045 {ECO:0000313|EMBL:OCX73355.1}, A6P07_11985
GN {ECO:0000313|EMBL:OCX71447.1};
OS Acidithiobacillus thiooxidans (Thiobacillus thiooxidans).
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=930 {ECO:0000313|EMBL:OCX71447.1, ECO:0000313|Proteomes:UP000094893};
RN [1] {ECO:0000313|Proteomes:UP000094893, ECO:0000313|Proteomes:UP000095008}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A02 {ECO:0000313|EMBL:OCX71447.1,
RC ECO:0000313|Proteomes:UP000094893}, and DXS-W
RC {ECO:0000313|EMBL:OCX73355.1, ECO:0000313|Proteomes:UP000095008};
RA Zhang X., Feng X., Tao J., Ma L., Xiao Y., Liang Y., Liu X., Yin H.;
RT "Comparative genomics of the extreme acidophile Acidithiobacillus
RT thiooxidans reveals intraspecific divergence and niche adaptation.";
RL Int. J. Mol. Sci. 0:0-0(2016).
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:OCX71447.1}.
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DR EMBL; LWSA01000167; OCX71447.1; -; Genomic_DNA.
DR EMBL; LWRY01000080; OCX73355.1; -; Genomic_DNA.
DR RefSeq; WP_024893443.1; NZ_LZYI01000266.1.
DR AlphaFoldDB; A0A1C2IN07; -.
DR STRING; 930.GCA_002079865_02587; -.
DR GeneID; 60694617; -.
DR eggNOG; COG0760; Bacteria.
DR OrthoDB; 14196at2; -.
DR Proteomes; UP000094893; Unassembled WGS sequence.
DR Proteomes; UP000095008; 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; 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; 2.
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 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..25
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01183"
FT CHAIN 26..479
FT /note="Chaperone SurA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01183"
FT /id="PRO_5009729370"
FT DOMAIN 218..319
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
FT DOMAIN 327..426
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 479 AA; 52685 MW; BEB346E0BC0B5E3A CRC64;
MSCKRRPLVI ALSLLLGTLP VAGWASTPFL NRDTLLAQAP APAVDSAPAT HTYSEDSALA
PMNAPMPSNA VNLDKIVAIV NDNIITSMQL EQRVSAVRAH LQQSDPNAMP ADDILRRQVL
QQMILQDIEL QMAQRANIKV DKGMLDQAVN NLAQANHMTA DQLRQALSSQ GQSWETFTND
LKDRIIVDRL MQQEVESRVH VGPDEVKTFA HQLKDMGGVS FNLQQIFIPM PNNPTPNAIS
TARQQATEVR NHLIAGEDFS RLAAQVSSGR DALQGGRIGW VKAGELPPSV SQALMSLKTG
DISQVIAGPT GFHIFKILDK KDEQPTITEV KAAAIVLRAG SSLQLQEAED RAQDIQTALQ
NGSRFSELAR NYSQDPNTAA KGGEMGWITP GQLPDTLERT LLTLQPGAVS SPIREGDAIY
ILQSQGRRQQ PVEEKQIMAA ARMQLFNRIV RERMDEWQHR IRDSAYVEIL EPNLRGSDA
//
