ID A0A259ERM3_9PROT Unreviewed; 436 AA.
AC A0A259ERM3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=B7X93_06660 {ECO:0000313|EMBL:OZA28898.1};
OS Hydrogenophilales bacterium 17-61-9.
OC Bacteria; Pseudomonadota; Hydrogenophilia; Hydrogenophilales.
OX NCBI_TaxID=1970524 {ECO:0000313|EMBL:OZA28898.1, ECO:0000313|Proteomes:UP000215711};
RN [1] {ECO:0000313|EMBL:OZA28898.1, ECO:0000313|Proteomes:UP000215711}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17-61-9 {ECO:0000313|EMBL:OZA28898.1};
RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT "Lifting the veil on microbial sulfur biogeochemistry in mining
RT wastewaters.";
RL Submitted (MAR-2017) 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}.
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:OZA28898.1}.
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DR EMBL; NCIF01000059; OZA28898.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A259ERM3; -.
DR Proteomes; UP000215711; 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; 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 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..30
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01183"
FT CHAIN 31..436
FT /note="Chaperone SurA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01183"
FT /id="PRO_5013416650"
FT DOMAIN 180..281
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
FT DOMAIN 291..389
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 436 AA; 48828 MW; D78E1B01BAC0FED3 CRC64;
MTIFKRPEWR RPLAMLVMLI AASASLPAQA AVTPLDHIVA VVNDEVITRQ ELARRYNEVT
QKLSKQNTPL PQRDVLEKQL LERMVTELAL QQHARSTGVR VDPTQTERAL QRIAAQNKLD
MAGLQAALTR DGMTLDSLRT TIRNEILIAR ARERDVDNRI SVSDAEIEGY LQTLTQQGVE
TEYNFAHILV TVPENASPEQ IQTRRARAED VLAQLAQGAD FAQLSASYSD APNALQGGGF
DWRASGKLPS LFVDTLKSMQ PGQTSPLLKS SNGFHILKLY DKRGLDATLN VTQTHARHIL
IKTNELTSES DARTRLLQLK ERIDNGVKFG ELAQLHSEDG SASKGGELGW VNPGDTVPDF
EQAMDALKPG EVSAPIQSPF GWHLIQVLER RNQDVTQERQ KLLARQAIRE RKAEEAFEDW
VRQIRDSAYV ELRPIN
//
