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Database: UniProt
Entry: A0A1K1P5K0_9GAMM
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ID   A0A1K1P5K0_9GAMM        Unreviewed;       457 AA.
AC   A0A1K1P5K0;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
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=SAMN02800691_1753 {ECO:0000313|EMBL:SFW42747.1};
OS   Luteibacter sp. UNCMF366Tsu5.1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Luteibacter.
OX   NCBI_TaxID=1502758 {ECO:0000313|EMBL:SFW42747.1, ECO:0000313|Proteomes:UP000182005};
RN   [1] {ECO:0000313|EMBL:SFW42747.1, ECO:0000313|Proteomes:UP000182005}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UNCMF366Tsu5.1 {ECO:0000313|EMBL:SFW42747.1,
RC   ECO:0000313|Proteomes:UP000182005};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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; FPIS01000001; SFW42747.1; -; Genomic_DNA.
DR   RefSeq; WP_072322027.1; NZ_FPIS01000001.1.
DR   AlphaFoldDB; A0A1K1P5K0; -.
DR   STRING; 1502758.SAMN02800691_1753; -.
DR   OrthoDB; 14196at2; -.
DR   Proteomes; UP000182005; 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|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:UP000182005};
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..23
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01183"
FT   CHAIN           24..457
FT                   /note="Chaperone SurA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01183"
FT                   /id="PRO_5013412366"
FT   DOMAIN          187..288
FT                   /note="PpiC"
FT                   /evidence="ECO:0000259|PROSITE:PS50198"
FT   DOMAIN          297..397
FT                   /note="PpiC"
FT                   /evidence="ECO:0000259|PROSITE:PS50198"
SQ   SEQUENCE   457 AA;  49885 MW;  909BFF36B518FF93 CRC64;
     MKQIFAYSLL AASILVAVPS AHAQLMPSAQ PAQGQGMSVG NGSLDRIVAV VEEDVILQSE
     LDEAINAIVR QYASNPGQLP PKDVLARQVL DRLILMKLQV QRANDQGIRV SDQDVDQAAA
     NVAQQNKMSL DQLRAAVEQD GYSYAAFRQQ LSDQIIAQKL HESVVRDQVT VTDAEVNNLL
     ASPTYKAGEV HLAHIQISTP AGGSASDIAQ AQAKAEEAIK AIKGGMDFNA AAIRYSDAPD
     ALDGGDLGWR RLDEVPPAFA DAIGSLKPGE TTAAMRGPTG FHILKLVETR QPGRQIVTEY
     HARQILIKPS EIVTPEQAEK KAEDLYTRIV DKHEDFAKLA KDESKDNTTA NNGGDMGWFA
     KDAWGQAIAT QIDQLKDNEV SHPIQTDAGW IVLQRLGTRQ SDLTDQLQRD QARQAIGNRK
     ADEAYENYLR ELRSTSFVDI RVPELKDPDD KQASATP
//
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