UniProtKB - P0ABZ6 (SURA_ECOLI)

BLAST

>sp|P0ABZ6|SURA_ECOLI Chaperone SurA OS=Escherichia coli (strain K12) OX=83333 GN=surA PE=1 SV=1
MKNWKTLLLGIAMIANTSFAAPQVVDKVAAVVNNGVVLESDVDGLMQSVKLNAAQARQQL
PDDATLRHQIMERLIMDQIILQMGQKMGVKISDEQLDQAIANIAKQNNMTLDQMRSRLAY
DGLNYNTYRNQIRKEMIISEVRNNEVRRRITILPQEVESLAQQVGNQNDASTELNLSHIL
IPLPENPTSDQVNEAESQARAIVDQARNGADFGKLAIAHSADQQALNGGQMGWGRIQELP
GIFAQALSTAKKGDIVGPIRSGVGFHILKVNDLRGESKNISVTEVHARHILLKPSPIMTD
EQARVKLEQIAADIKSGKTTFAAAAKEFSQDPGSANQGGDLGWATPDIFDPAFRDALTRL
NKGQMSAPVHSSFGWHLIELLDTRNVDKTDAAQKDRAYRMLMNRKFSEEAASWMQEQRAS
AYVKILSN

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History
Entry version 109 (28 Mar 2018)
Sequence version 1 (08 Nov 2005)
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Protein

Chaperone SurA

Gene

surA

Organism

Escherichia coli (strain K12)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

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.3 Publications

Catalytic activityⁱ

Peptidylproline (omega=180) = peptidylproline (omega=0).

GO - Molecular functionⁱ

peptide binding
Source: EcoCyc
Inferred from direct assayⁱ
peptidyl-prolyl cis-trans isomerase activity
Source: EcoCyc
Inferred from direct assayⁱ
- 8985185
unfolded protein binding
Source: EcoCyc
Inferred from physical interactionⁱ
- 11226178

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

chaperone cofactor-dependent protein refolding
Source: EcoCyc
Inferred from mutant phenotypeⁱ
- 17071751
Gram-negative-bacterium-type cell outer membrane assembly
Source: EcoliWiki
Inferred from mutant phenotypeⁱ
- 8985185
maintenance of stationary phase
Source: EcoliWiki
Inferred from mutant phenotypeⁱ
- 2165476
protein folding
Source: EcoCyc
Inferred from mutant phenotypeⁱ
protein stabilization
Source: EcoCyc
Inferred from direct assayⁱ
- 11226178

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Chaperone, Isomerase, Rotamase

Molecular function

Chaperone, Isomerase, Rotamase

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG10985-MONOMER MetaCyc:EG10985-MONOMER

BioCycⁱ

EcoCyc:EG10985-MONOMER
MetaCyc:EG10985-MONOMER

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Chaperone SurA Alternative name(s): Peptidyl-prolyl cis-trans isomerase SurA (EC:5.2.1.8) Short name: PPIase SurA Rotamase SurA Survival protein A
Gene namesⁱ	Name:surA Ordered Locus Names:b0053, JW0052
Organismⁱ	Escherichia coli (strain K12)
Taxonomic identifierⁱ	83333 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli
Proteomesⁱ	UP000000318 Componentⁱ: Chromosome UP000000625 Componentⁱ: Chromosome

Organism-specific databases

EcoGeneⁱ	EG10985 surA

EcoGeneⁱ

EG10985 surA

Subcellular locationⁱ

Periplasm

Note:

Is capable of associating with the outer membrane.

GO - Cellular componentⁱ

outer membrane-bounded periplasmic space
Source: EcoCyc
Inferred from direct assayⁱ
- 15911532
- 24140104

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Periplasm

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Signal peptideⁱ	1 – 20	3 PublicationsAdd BLAST		20
ChainⁱPRO_0000025542	21 – 428	Chaperone SurAAdd BLAST		408

Proteomic databases

EPDⁱ	P0ABZ6
PaxDbⁱ	P0ABZ6
PRIDEⁱ	P0ABZ6

2D gel databases

SWISS-2DPAGEⁱ	P0ABZ6

SWISS-2DPAGEⁱ

P0ABZ6

Interactionⁱ

Binary interactionsⁱ

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

With

Entry

#Exp.

IntAct

Notes

bamB

P77774

EBI-558651,EBI-907297

GO - Molecular functionⁱ

unfolded protein binding
Source: EcoCyc
Inferred from physical interactionⁱ
- 11226178

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	4261014, 418 interactors
Database of interacting proteins More...DIPⁱ	DIP-35827N
IntActⁱ	P0ABZ6, 10 interactors
STRINGⁱ	316385.ECDH10B_0054

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	28 – 38	Combined sources	11
Helixⁱ	39 – 54	Combined sources	16
Turnⁱ	55 – 57	Combined sources	3
Helixⁱ	63 – 86	Combined sources	24
Helixⁱ	93 – 106	Combined sources	14
Helixⁱ	111 – 121	Combined sources	11
Helixⁱ	125 – 148	Combined sources	24
Helixⁱ	156 – 162	Combined sources	7
Beta strandⁱ	173 – 182	Combined sources	10
Helixⁱ	189 – 207	Combined sources	19
Helixⁱ	212 – 219	Combined sources	8
Helixⁱ	225 – 227	Combined sources	3
Beta strandⁱ	230 – 234	Combined sources	5
Helixⁱ	236 – 238	Combined sources	3
Helixⁱ	241 – 246	Combined sources	6
Turnⁱ	247 – 249	Combined sources	3
Beta strandⁱ	255 – 261	Combined sources	7
Beta strandⁱ	264 – 274	Combined sources	11
Beta strandⁱ	282 – 292	Combined sources	11
Beta strandⁱ	296 – 298	Combined sources	3
Helixⁱ	300 – 315	Combined sources	16
Helixⁱ	321 – 328	Combined sources	8
Turnⁱ	332 – 334	Combined sources	3
Helixⁱ	335 – 337	Combined sources	3
Beta strandⁱ	340 – 344	Combined sources	5
Helixⁱ	346 – 348	Combined sources	3
Helixⁱ	351 – 358	Combined sources	8
Beta strandⁱ	375 – 386	Combined sources	12
Helixⁱ	396 – 420	Combined sources	25
Beta strandⁱ	423 – 425	Combined sources	3

Show more details

3D structure databases

ProteinModelPortalⁱ	P0ABZ6
SMRⁱ	P0ABZ6
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P0ABZ6

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	171 – 272	PpiC 1Add BLAST		102
Domainⁱ	282 – 382	PpiC 2Add BLAST		101

Domainⁱ

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.1 Publication

Keywords - Domainⁱ

Repeat, Signal

Phylogenomic databases

eggNOGⁱ	ENOG4105DBD Bacteria COG0760 LUCA
HOGENOMⁱ	HOG000264337
InParanoidⁱ	P0ABZ6
KEGG Orthology (KO) More...KOⁱ	K03771
OMAⁱ	EMIISRV
PhylomeDBⁱ	P0ABZ6

Family and domain databases

HAMAPⁱ	MF_01183 Chaperone_SurA, 1 hit
InterProⁱ	View protein in InterPro IPR000297 PPIase_PpiC IPR023058 PPIase_PpiC_CS IPR023034 PPIase_SurA IPR015391 SurA_N IPR027304 Trigger_fact/SurA_dom_sf
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00639 Rotamase, 1 hit PF09312 SurA_N, 1 hit
SUPFAMⁱ	SSF109998 SSF109998, 1 hit
PROSITEⁱ	View protein in PROSITE PS01096 PPIC_PPIASE_1, 2 hits PS50198 PPIC_PPIASE_2, 2 hits

Sequenceⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

P0ABZ6-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MKNWKTLLLG IAMIANTSFA APQVVDKVAA VVNNGVVLES DVDGLMQSVK 
        60         70         80         90        100
LNAAQARQQL PDDATLRHQI MERLIMDQII LQMGQKMGVK ISDEQLDQAI 
       110        120        130        140        150
ANIAKQNNMT LDQMRSRLAY DGLNYNTYRN QIRKEMIISE VRNNEVRRRI 
       160        170        180        190        200
TILPQEVESL AQQVGNQNDA STELNLSHIL IPLPENPTSD QVNEAESQAR 
       210        220        230        240        250
AIVDQARNGA DFGKLAIAHS ADQQALNGGQ MGWGRIQELP GIFAQALSTA 
       260        270        280        290        300
KKGDIVGPIR SGVGFHILKV NDLRGESKNI SVTEVHARHI LLKPSPIMTD 
       310        320        330        340        350
EQARVKLEQI AADIKSGKTT FAAAAKEFSQ DPGSANQGGD LGWATPDIFD 
       360        370        380        390        400
PAFRDALTRL NKGQMSAPVH SSFGWHLIEL LDTRNVDKTD AAQKDRAYRM 
       410        420 
LMNRKFSEEA ASWMQEQRAS AYVKILSN

Length:428

Mass (Da):47,284

Last modified:November 8, 2005 - v1

Checksum:ⁱ25F6AD4B903CBD8E

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	25	V → D (Ref. 1) Curated	1
Sequence conflictⁱ	116	S → T (Ref. 1) Curated	1
Sequence conflictⁱ	213	G → GFG (Ref. 1) Curated	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U00096 Genomic DNA Translation: AAC73164.1 AP009048 Genomic DNA Translation: BAB96620.2 M68521 Genomic DNA Translation: AAA24304.1 AB013134 Genomic DNA Translation: BAA34131.1
PIRⁱ	E64726
NCBI Reference Sequences More...RefSeqⁱ	NP_414595.1, NC_000913.3 WP_000800457.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC73164; AAC73164; b0053 BAB96620; BAB96620; BAB96620
GeneIDⁱ	944812
KEGGⁱ	ecj:JW0052 eco:b0053
PATRICⁱ	fig\|1411691.4.peg.2230

Protein	Similar proteins		Species	Score	Length	Source
P0ABZ6	Chaperone SurA		ECO57		428	UniRef100_P0ABZ8
Chaperone SurA		ECOL6		428
Chaperone SurA		ECOUT		428
Chaperone SurA		SHIBS		428
Chaperone SurA		SHIFL		428
+163

Protein	Similar proteins		Species	Score	Length	Source
P0ABZ6	Chaperone SurA		ECO57		428	UniRef90_P0ABZ8
Chaperone SurA		ECOL6		428
Chaperone SurA		ECOUT		428
Chaperone SurA		SHIBS		428
Chaperone SurA		SHIFL		428
+584

Protein	Similar proteins		Species	Score	Length	Source
P0ABZ6	Chaperone SurA		ECO57		428	UniRef50_P0ABZ8
Chaperone SurA		ECOL6		428
Chaperone SurA		ECOUT		428
Chaperone SurA		SHIBS		428
Chaperone SurA		SHIFL		428
+1718

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U00096 Genomic DNA Translation: AAC73164.1 AP009048 Genomic DNA Translation: BAB96620.2 M68521 Genomic DNA Translation: AAA24304.1 AB013134 Genomic DNA Translation: BAA34131.1
PIRⁱ	E64726
RefSeqⁱ	NP_414595.1, NC_000913.3 WP_000800457.1, NZ_LN832404.1

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB 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	[»]
ProteinModelPortalⁱ	P0ABZ6
SMRⁱ	P0ABZ6
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4261014, 418 interactors
DIPⁱ	DIP-35827N
IntActⁱ	P0ABZ6, 10 interactors
STRINGⁱ	316385.ECDH10B_0054

2D gel databases

SWISS-2DPAGEⁱ	P0ABZ6

SWISS-2DPAGEⁱ

P0ABZ6

Proteomic databases

EPDⁱ	P0ABZ6
PaxDbⁱ	P0ABZ6
PRIDEⁱ	P0ABZ6

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC73164; AAC73164; b0053 BAB96620; BAB96620; BAB96620
GeneIDⁱ	944812
KEGGⁱ	ecj:JW0052 eco:b0053
PATRICⁱ	fig\|1411691.4.peg.2230

Organism-specific databases

EchoBASEⁱ	EB0978
EcoGeneⁱ	EG10985 surA

Phylogenomic databases

eggNOGⁱ	ENOG4105DBD Bacteria COG0760 LUCA
HOGENOMⁱ	HOG000264337
InParanoidⁱ	P0ABZ6
KOⁱ	K03771
OMAⁱ	EMIISRV
PhylomeDBⁱ	P0ABZ6

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG10985-MONOMER MetaCyc:EG10985-MONOMER

BioCycⁱ

EcoCyc:EG10985-MONOMER
MetaCyc:EG10985-MONOMER

Miscellaneous databases

EvolutionaryTraceⁱ	P0ABZ6
Protein Ontology More...PROⁱ	PR:P0ABZ6

Family and domain databases

HAMAPⁱ	MF_01183 Chaperone_SurA, 1 hit
InterProⁱ	View protein in InterPro IPR000297 PPIase_PpiC IPR023058 PPIase_PpiC_CS IPR023034 PPIase_SurA IPR015391 SurA_N IPR027304 Trigger_fact/SurA_dom_sf
Pfamⁱ	View protein in Pfam PF00639 Rotamase, 1 hit PF09312 SurA_N, 1 hit
SUPFAMⁱ	SSF109998 SSF109998, 1 hit
PROSITEⁱ	View protein in PROSITE PS01096 PPIC_PPIASE_1, 2 hits PS50198 PPIC_PPIASE_2, 2 hits
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	SURA_ECOLI
Accessionⁱ	P0ABZ6Primary (citable) accession number: P0ABZ6 Secondary accession number(s): P21202 , P75630, Q8KIP6, Q8KMY0
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	November 8, 2005
	Last sequence update:	November 8, 2005
	Last modified:	March 28, 2018
	This is version 109 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Escherichia coli
Escherichia coli (strain K12): entries and cross-references to EcoGene

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P0ABZ6 (SURA_ECOLI)

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Chaperone SurA

surA

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

2D gel databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Keywords - Cellular componentⁱ

PTM / Processingⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ