FKBA_ECOLI
ID FKBA_ECOLI Reviewed; 270 AA.
AC P45523; P39175; Q2M712;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=FKBP-type peptidyl-prolyl cis-trans isomerase FkpA;
DE Short=PPIase;
DE EC=5.2.1.8;
DE AltName: Full=Rotamase;
DE Flags: Precursor;
GN Name=fkpA; Synonyms=yzzS; OrderedLocusNames=b3347, JW3309;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / CS109;
RX PubMed=7540828; DOI=10.1007/bf00404209;
RA Horne S.M., Young K.D.;
RT "Escherichia coli and other species of the Enterobacteriaceae encode a
RT protein similar to the family of Mip-like FK506-binding proteins.";
RL Arch. Microbiol. 163:357-365(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP PROTEIN SEQUENCE OF 26-37.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [5]
RP CHARACTERIZATION.
RX PubMed=8878048; DOI=10.1046/j.1365-2958.1996.561412.x;
RA Missiakas D., Betton J.-M., Raina S.;
RT "New components of protein folding in extracytoplasmic compartments of
RT Escherichia coli SurA, FkpA and Skp/OmpH.";
RL Mol. Microbiol. 21:871-884(1996).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides.
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;
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L28082; AAC41459.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58144.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76372.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77944.1; -; Genomic_DNA.
DR PIR; I65035; I65035.
DR RefSeq; NP_417806.1; NC_000913.3.
DR RefSeq; WP_000838250.1; NZ_SSZK01000008.1.
DR PDB; 1Q6H; X-ray; 1.97 A; A/B=26-249.
DR PDB; 1Q6I; X-ray; 2.25 A; A/B=26-249.
DR PDB; 1Q6U; X-ray; 2.45 A; A=26-270.
DR PDB; 4QCC; X-ray; 7.08 A; A/B=45-116.
DR PDBsum; 1Q6H; -.
DR PDBsum; 1Q6I; -.
DR PDBsum; 1Q6U; -.
DR PDBsum; 4QCC; -.
DR AlphaFoldDB; P45523; -.
DR BMRB; P45523; -.
DR SMR; P45523; -.
DR BioGRID; 4263165; 57.
DR DIP; DIP-9625N; -.
DR IntAct; P45523; 17.
DR MINT; P45523; -.
DR STRING; 511145.b3347; -.
DR SWISS-2DPAGE; P45523; -.
DR jPOST; P45523; -.
DR PaxDb; P45523; -.
DR PRIDE; P45523; -.
DR EnsemblBacteria; AAC76372; AAC76372; b3347.
DR EnsemblBacteria; BAE77944; BAE77944; BAE77944.
DR GeneID; 947850; -.
DR KEGG; ecj:JW3309; -.
DR KEGG; eco:b3347; -.
DR PATRIC; fig|1411691.4.peg.3384; -.
DR EchoBASE; EB2737; -.
DR eggNOG; COG0545; Bacteria.
DR HOGENOM; CLU_013615_0_2_6; -.
DR InParanoid; P45523; -.
DR OMA; KYMSGHI; -.
DR PhylomeDB; P45523; -.
DR BioCyc; EcoCyc:G7716-MON; -.
DR BRENDA; 5.2.1.8; 2026.
DR EvolutionaryTrace; P45523; -.
DR PRO; PR:P45523; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:CACAO.
DR GO; GO:0042026; P:protein refolding; IDA:EcoliWiki.
DR DisProt; DP02787; -.
DR Gene3D; 1.10.287.460; -; 1.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR InterPro; IPR000774; PPIase_FKBP_N.
DR InterPro; IPR036944; PPIase_FKBP_N_sf.
DR Pfam; PF00254; FKBP_C; 1.
DR Pfam; PF01346; FKBP_N; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Isomerase; Periplasm;
KW Reference proteome; Rotamase; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:9298646"
FT CHAIN 26..270
FT /note="FKBP-type peptidyl-prolyl cis-trans isomerase FkpA"
FT /id="PRO_0000025536"
FT DOMAIN 164..249
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT HELIX 44..68
FT /evidence="ECO:0007829|PDB:1Q6H"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:1Q6H"
FT HELIX 76..87
FT /evidence="ECO:0007829|PDB:1Q6H"
FT HELIX 95..137
FT /evidence="ECO:0007829|PDB:1Q6H"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:1Q6H"
FT STRAND 149..154
FT /evidence="ECO:0007829|PDB:1Q6H"
FT STRAND 166..175
FT /evidence="ECO:0007829|PDB:1Q6H"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:1Q6H"
FT HELIX 184..187
FT /evidence="ECO:0007829|PDB:1Q6H"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:1Q6H"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:1Q6H"
FT HELIX 200..205
FT /evidence="ECO:0007829|PDB:1Q6H"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:1Q6H"
FT STRAND 214..219
FT /evidence="ECO:0007829|PDB:1Q6H"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:1Q6H"
FT TURN 224..228
FT /evidence="ECO:0007829|PDB:1Q6H"
FT STRAND 239..249
FT /evidence="ECO:0007829|PDB:1Q6H"
SQ SEQUENCE 270 AA; 28882 MW; DBC73B8676BB63EF CRC64;
MKSLFKVTLL ATTMAVALHA PITFAAEAAK PATAADSKAA FKNDDQKSAY ALGASLGRYM
ENSLKEQEKL GIKLDKDQLI AGVQDAFADK SKLSDQEIEQ TLQAFEARVK SSAQAKMEKD
AADNEAKGKE YREKFAKEKG VKTSSTGLVY QVVEAGKGEA PKDSDTVVVN YKGTLIDGKE
FDNSYTRGEP LSFRLDGVIP GWTEGLKNIK KGGKIKLVIP PELAYGKAGV PGIPPNSTLV
FDVELLDVKP APKADAKPEA DAKAADSAKK
