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Database: UniProt
Entry: A0A0L7TAA7_9GAMM
LinkDB: A0A0L7TAA7_9GAMM
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ID   A0A0L7TAA7_9GAMM        Unreviewed;       431 AA.
AC   A0A0L7TAA7;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 42.
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=NG42_14610 {ECO:0000313|EMBL:KOC88945.1}, NG43_14095
GN   {ECO:0000313|EMBL:KOC92314.1};
OS   Erwinia iniecta.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=1560201 {ECO:0000313|EMBL:KOC92314.1, ECO:0000313|Proteomes:UP000036851};
RN   [1] {ECO:0000313|Proteomes:UP000036851, ECO:0000313|Proteomes:UP000037088}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B120 {ECO:0000313|EMBL:KOC88945.1,
RC   ECO:0000313|Proteomes:UP000037088}, and B149
RC   {ECO:0000313|EMBL:KOC92314.1, ECO:0000313|Proteomes:UP000036851};
RX   PubMed=26198254;
RA   Campillo T., Luna E., Portier P., Fischer-Le Saux M., Lapitan N.,
RA   Tisserat N.A., Leach J.E.;
RT   "Erwinia iniecta sp. nov., isolated from Russian wheat aphids (Diuraphis
RT   noxia).";
RL   Int. J. Syst. Evol. Microbiol. 0:0-0(2015).
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:KOC92314.1}.
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DR   EMBL; JRXE01000020; KOC88945.1; -; Genomic_DNA.
DR   EMBL; JRXF01000021; KOC92314.1; -; Genomic_DNA.
DR   RefSeq; WP_052900334.1; NZ_JRXF01000021.1.
DR   AlphaFoldDB; A0A0L7TAA7; -.
DR   STRING; 1560201.NG42_14610; -.
DR   PATRIC; fig|1560201.3.peg.3104; -.
DR   OrthoDB; 14196at2; -.
DR   Proteomes; UP000036851; Unassembled WGS sequence.
DR   Proteomes; UP000037088; 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; 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   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|HAMAP-Rule:MF_01183, ECO:0000256|PROSITE-
KW   ProRule:PRU00278};
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764, ECO:0000256|HAMAP-Rule:MF_01183};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037088};
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..20
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01183"
FT   CHAIN           21..431
FT                   /note="Chaperone SurA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01183"
FT                   /id="PRO_5011013211"
FT   DOMAIN          171..272
FT                   /note="PpiC"
FT                   /evidence="ECO:0000259|PROSITE:PS50198"
FT   DOMAIN          282..382
FT                   /note="PpiC"
FT                   /evidence="ECO:0000259|PROSITE:PS50198"
SQ   SEQUENCE   431 AA;  47474 MW;  F7D7D23DC35F8F70 CRC64;
     MKNWRTLILG VALAANTAFA APQVVDKVAA VVNNGVVLES DVNGMMQSVK AQAQQAGQQL
     PDDKTLRHQI VERQIMDNIL LQMGKQMGVQ ITDQQLDQAI GNIAAQNHMS MDQMRSRLAY
     DGVNYGTYRE QIRKEMLIAE VRNNEVRRRV TILPQEVDTL ATQVGAQNNR GTELNLSHIL
     LPLPENPTQQ QVDDQENLAK QLVGEIKGGA DFGKLAVTYS ADSQALKGGN MGWGKIEELP
     TLFAQALSTA KKGDIVGPIR SGVGFHILKV NDLRGESQNI SVTEVHARHI LLKPSPVLTD
     AQARQKLEQV AADIQSGKTD FASAAKQLSD DPGSANQGGD LGWTSAEVFD PAFRDALLKL
     NKGQLSQPVH SSFGWHLIQL LDTRQVDKTD AAQKERAYRL LFNRKFAEEA QTWMQEQRAS
     AYVKILDQNA Q
//
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