P0ABZ6 (SURA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Chaperone SurA

Alternative name(s):
Peptidyl-prolyl cis-trans isomerase SurA
Short name=PPIase SurA
EC=5.2.1.8
Rotamase SurA
Survival protein A

Gene names

Name:	surA
Ordered Locus Names:	b0053, JW0052

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	428 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Chaperone involved in the correct folding and assembly of outer membrane proteins, such as OmpA, OmpF and LamB. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associated steps of protein maturation. Essential for the survival of E.coli in stationary phase. Required for pilus biogenesis. Ref.10 Ref.12 Ref.13 Ref.16
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0). HAMAP-Rule MF_01183
Subcellular location	Periplasm. Note: Is capable of associating with the outer membrane. HAMAP-Rule MF_01183
Domain	The PPIase activity resides only in the second parvulin domain. The N-terminal region and the C-terminal tail are necessary and sufficient for the chaperone activity of SurA. The PPIase activity is dispensable for SurA function as a SurA protein with a deletion of the parvulin domains is almost completely functional in vivo. The N-terminal region and the C-terminal tail are also required for porin recognition. Ref.13
Sequence similarities	Contains 2 PpiC domains.

Ontologies

Keywords
Cellular component	Periplasm
Domain	Repeat Signal
Molecular function	Chaperone Isomerase Rotamase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	Gram-negative-bacterium-type cell outer membrane assembly Inferred from mutant phenotype Ref.12. Source: EcoliWiki biofilm formation Inferred from mutant phenotype PubMed 18180259. Source: EcoCyc chaperone mediated protein folding requiring cofactor Inferred from mutant phenotype PubMed 17071751. Source: EcoCyc maintenance of stationary phase Inferred from mutant phenotype Ref.10. Source: EcoliWiki protein stabilization Inferred from direct assay Ref.13. Source: EcoCyc
Cellular_component	outer membrane-bounded periplasmic space Inferred from direct assay Ref.12. Source: EcoliWiki
Molecular_function	peptide binding Inferred from direct assay PubMed 11546789Ref.14Ref.15PubMed 17825319PubMed 17894549. Source: EcoCyc peptidyl-prolyl cis-trans isomerase activity Inferred from direct assay Ref.12. Source: EcoCyc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
bamB	P77774	2	EBI-558651,EBI-907297

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

20

Ref.7 Ref.8 Ref.9

Chain

21 – 428

408

Chaperone SurA HAMAP-Rule MF_01183

PRO_0000025542

Regions

Domain

171 – 272

102

PpiC 1

Domain

282 – 382

101

PpiC 2

Experimental info

Sequence conflict

25

1

V → D Ref.1

Sequence conflict

116

1

S → T Ref.1

Sequence conflict

213

1

G → GFG Ref.1

Secondary structure

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428

Helix Strand Turn

Details...

Beta strand

28 – 38

11

Helix

39 – 54

16

Turn

55 – 57

3

Helix

63 – 86

24

Helix

93 – 106

14

Helix

111 – 121

11

Helix

125 – 148

24

Helix

156 – 162

7

Beta strand

173 – 182

10

Helix

189 – 207

19

Helix

212 – 219

8

Helix

225 – 227

3

Beta strand

230 – 234

5

Helix

236 – 238

3

Helix

241 – 246

6

Turn

247 – 249

3

Beta strand

255 – 261

7

Beta strand

264 – 274

11

Beta strand

282 – 292

11

Beta strand

296 – 298

3

Helix

300 – 315

16

Helix

321 – 328

8

Turn

332 – 334

3

Helix

335 – 337

3

Beta strand

340 – 344

5

Helix

346 – 348

3

Helix

351 – 358

8

Beta strand

375 – 386

12

Helix

396 – 420

25

Beta strand

423 – 425

3

Sequences

	Sequence		Length	Mass (Da)
	P0ABZ6 [UniParc]. Last modified November 8, 2005. Version 1. Checksum: 25F6AD4B903CBD8E	FASTA	428	47,284
	10 20 30 40 50 60 MKNWKTLLLG IAMIANTSFA APQVVDKVAA VVNNGVVLES DVDGLMQSVK LNAAQARQQL 70 80 90 100 110 120 PDDATLRHQI MERLIMDQII LQMGQKMGVK ISDEQLDQAI ANIAKQNNMT LDQMRSRLAY 130 140 150 160 170 180 DGLNYNTYRN QIRKEMIISE VRNNEVRRRI TILPQEVESL AQQVGNQNDA STELNLSHIL 190 200 210 220 230 240 IPLPENPTSD QVNEAESQAR AIVDQARNGA DFGKLAIAHS ADQQALNGGQ MGWGRIQELP 250 260 270 280 290 300 GIFAQALSTA KKGDIVGPIR SGVGFHILKV NDLRGESKNI SVTEVHARHI LLKPSPIMTD 310 320 330 340 350 360 EQARVKLEQI AADIKSGKTT FAAAAKEFSQ DPGSANQGGD LGWATPDIFD PAFRDALTRL 370 380 390 400 410 420 NKGQMSAPVH SSFGWHLIEL LDTRNVDKTD AAQKDRAYRM LMNRKFSEEA ASWMQEQRAS AYVKILSN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Almiron M., Tormo A., Kolter R. Unpublished observations (JAN-1993) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region." Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A. Nucleic Acids Res. 20:3305-3308(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Overlap between pdxA and ksgA in the complex pdxA-ksgA-apaG-apaH operon of Escherichia coli K-12." Roa B.B., Connolly D.M., Winkler M.E. J. Bacteriol. 171:4767-4777(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 331-428. Strain: K12.
[6]	"N-hexane sensitivity of Escherichia coli due to low expression of ostA/imp by insertion of IS2 and identification of the gene product as an outer membrane protein." Abe S., Okutsu T., Negishi T., Nakajima H., Aono R. Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 21-32. Strain: K12 / EMG2.
[8]	"SurA assists the folding of Escherichia coli outer membrane proteins." Lazar S.W., Kolter R. J. Bacteriol. 178:1770-1773(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 21-30, CHARACTERIZATION.
[9]	"Protein identification with N and C-terminal sequence tags in proteome projects." Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C., Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L., Hochstrasser D.F. J. Mol. Biol. 278:599-608(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 21-24. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[10]	"surA, an Escherichia coli gene essential for survival in stationary phase." Tormo A., Almiron M., Kolter R. J. Bacteriol. 172:4339-4347(1990) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[11]	"New components of protein folding in extracytoplasmic compartments of Escherichia coli SurA, FkpA and Skp/OmpH." Missiakas D., Betton J.-M., Raina S. Mol. Microbiol. 21:871-884(1996) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[12]	"SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins." Rouviere P.E., Gross C.A. Genes Dev. 10:3170-3182(1996) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[13]	"The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity." Behrens S., Maier R., de Cock H., Schmid F.X., Gross C.A. EMBO J. 20:285-294(2001) [PubMed] [Europe PMC] [Abstract] Cited for: DOMAIN FUNCTION.
[14]	"The periplasmic molecular chaperone protein SurA binds a peptide motif that is characteristic of integral outer membrane proteins." Bitto E., McKay D.B. J. Biol. Chem. 278:49316-49322(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBSTRATE RECOGNITION.
[15]	"The periplasmic chaperone SurA exploits two features characteristic of integral outer membrane proteins for selective substrate recognition." Hennecke G., Nolte J., Volkmer-Engert R., Schneider-Mergener J., Behrens S. J. Biol. Chem. 280:23540-23548(2005) [PubMed] [Europe PMC] [Abstract] Cited for: SUBSTRATE RECOGNITION.
[16]	"Periplasmic peptidyl prolyl cis-trans isomerases are not essential for viability, but SurA is required for pilus biogenesis in Escherichia coli." Justice S.S., Hunstad D.A., Harper J.R., Duguay A.R., Pinkner J.S., Bann J., Frieden C., Silhavy T.J., Hultgren S.J. J. Bacteriol. 187:7680-7686(2005) [PubMed] [Europe PMC] [Abstract] Cited for: ROLE IN PILUS BIOGENESIS. Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[17]	"Crystallographic structure of SurA, a molecular chaperone that facilitates folding of outer membrane porins." Bitto E., McKay D.B. Structure 10:1489-1498(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 21-428.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U00096 Genomic DNA. Translation: AAC73164.1.
AP009048 Genomic DNA. Translation: BAB96620.2.
M68521 Genomic DNA. Translation: AAA24304.1.
AB013134 Genomic DNA. Translation: BAA34131.1.

PIR

E64726.

RefSeq

NP_414595.1. NC_000913.2.
YP_488359.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1M5Y	X-ray	3.00	A/B/C/D	21-428	[»]
2PV1	X-ray	1.30	A	172-274	[»]
2PV2	X-ray	1.30	A/B/C/D	172-274	[»]
2PV3	X-ray	3.39	A/B	21-428	[»]

ProteinModelPortal

P0ABZ6.

SMR

P0ABZ6. Positions 25-428.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35827N.

IntAct

P0ABZ6. 10 interactions.

MINT

MINT-1242178.

STRING

511145.b0053.

2D gel databases

SWISS-2DPAGE

P0ABZ6.

Proteomic databases

PaxDb

P0ABZ6.

PRIDE

P0ABZ6.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC73164; AAC73164; b0053.
BAB96620; BAB96620; BAB96620.

GeneID

12932020.
944812.

KEGG

ecj:Y75_p0053.
eco:b0053.

PATRIC

32115205. VBIEscCol129921_0054.

Organism-specific databases

EchoBASE

EB0978.

EcoGene

EG10985. surA.

Phylogenomic databases

eggNOG

COG0760.

HOGENOM

HOG000264337.

KO

K03771.

OMA

FGVHLIQ.

ProtClustDB

PRK10770.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10985-MONOMER.
ECOL316407:JW0052-MONOMER.
MetaCyc:EG10985-MONOMER.

Gene expression databases

Genevestigator

P0ABZ6.

Family and domain databases

HAMAP

MF_01183. Chaperone_SurA.

InterPro

IPR000297. PPIase_PpiC.
IPR023058. PPIase_PpiC_CS.
IPR023034. PPIase_SurA.
IPR015391. SurA_N.
IPR027304. Trigger_fact/SurA_dom.
[Graphical view]

Pfam

PF00639. Rotamase. 2 hits.
PF09312. SurA_N. 1 hit.
[Graphical view]

SUPFAM

SSF109998. Trigger_fac_C_bac. 1 hit.

PROSITE

PS01096. PPIC_PPIASE_1. 2 hits.
PS50198. PPIC_PPIASE_2. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0ABZ6.

Entry information

Entry name

SURA_ECOLI

Accession

Primary (citable) accession number: P0ABZ6
Secondary accession number(s): P21202 , P75630, Q8KIP6, Q8KMY0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2005
Last sequence update:	November 8, 2005
Last modified:	May 1, 2013
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program