P35160 (RESA_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Thiol-disulfide oxidoreductase ResA

Gene names

Name:	resA
Synonyms:	ypxA
Ordered Locus Names:	BSU23150

Organism

Bacillus subtilis (strain 168) [Reference proteome] [HAMAP]

Taxonomic identifier

224308 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group › Bacillus subtilis › Bacillus subtilis subsp. subtilis

Protein attributes

Sequence length	179 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Thiol-disulfide oxidoreductase which is required in disulfide reduction during c-type cytochrome synthesis. May accept reducing equivalents from CcdA, leading to breakage of disulfide bonds in apocytochrome c; following this reduction heme can be covalently attached. Does not play a role in sporulation. Ref.5
Pathway	Protein modification; cytochrome c assembly. HAMAP-Rule MF_01319
Subcellular location	Cell membrane; Single-pass type II membrane protein. Note: The thioredoxin-like motif is exposed on the outside of the membrane. Ref.5
Sequence similarities	Belongs to the thioredoxin family. ResA subfamily. Contains 1 thioredoxin domain.
Sequence caution	The sequence AAA67494.1 differs from that shown. Reason: Frameshift at position 39.

Ontologies

Keywords
Biological process	Cytochrome c-type biogenesis
Cellular component	Cell membrane Membrane
Domain	Redox-active center Signal-anchor Transmembrane Transmembrane helix
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell redox homeostasis Inferred from electronic annotation. Source: HAMAP cytochrome complex assembly Inferred from electronic annotation. Source: HAMAP
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	antioxidant activity Inferred from electronic annotation. Source: InterPro disulfide oxidoreductase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 179

179

Thiol-disulfide oxidoreductase ResA HAMAP-Rule MF_01319

PRO_0000120149

Regions

Transmembrane

11 – 30

20

Helical; Signal-anchor for type II membrane protein; Probable

Domain

36 – 174

139

Thioredoxin

Amino acid modifications

Disulfide bond

74 ↔ 77

Redox-active HAMAP-Rule MF_01319

Secondary structure

1

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179

Helix Strand Turn

Details...

Beta strand

46 – 48

3

Beta strand

54 – 56

3

Helix

57 – 60

4

Beta strand

63 – 70

8

Helix

75 – 91

17

Helix

92 – 94

3

Beta strand

96 – 104

9

Helix

107 – 117

11

Beta strand

123 – 126

4

Helix

130 – 134

5

Beta strand

142 – 146

5

Beta strand

150 – 158

9

Helix

162 – 172

11

Sequences

	Sequence		Length	Mass (Da)
	P35160 [UniParc]. Last modified August 29, 2003. Version 2. Checksum: E023A46F4BD702AC	FASTA	179	20,008
	10 20 30 40 50 60 MKKKRRLFIR TGILLVLICA LGYTIYNAVF AGKESISEGS DAPNFVLEDT NGKRIELSDL 70 80 90 100 110 120 KGKGVFLNFW GTWCEPCKKE FPYMANQYKH FKSQGVEIVA VNVGESKIAV HNFMKSYGVN 130 140 150 160 170 FPVVLDTDRQ VLDAYDVSPL PTTFLINPEG KVVKVVTGTM TESMIHDYMN LIKPGETSG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The organization of the Bacillus subtilis 168 chromosome region between the spoVA and serA genetic loci, based on sequence data." Sorokin A.V., Zumstein E., Azevedo V., Ehrlich S.D., Serror P. Mol. Microbiol. 10:385-395(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
[2]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[3]	"From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later." Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A. Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION.
[4]	"Regulators of aerobic and anaerobic respiration in Bacillus subtilis." Sun G., Sharkova E., Chesnut R., Birkey S., Duggan M.F., Sorokin A.V., Pujic P., Ehrlich S.D., Hulett F.M. J. Bacteriol. 178:1374-1385(1996) [PubMed] [Europe PMC] [Abstract] Cited for: GENE NAME.
[5]	"Bacillus subtilis ResA is a thiol-disulfide oxidoreductase involved in cytochrome c synthesis." Erlendsson L.S., Acheson R.M., Hederstedt L., Le Brun N.E. J. Biol. Chem. 278:17852-17858(2003) [PubMed] [Europe PMC] [Abstract] Cited for: DETECTION OF FRAMESHIFT, FUNCTION, SUBCELLULAR LOCATION. Strain: 168 / BGSC1A1.
[6]	"Structural basis of redox-coupled protein substrate selection by the cytochrome c biosynthesis protein ResA." Crow A., Acheson R.M., Le Brun N.E., Oubrie A. J. Biol. Chem. 279:23654-23660(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 37-179 IN THE OXIDIZED AND REDUCED STATES. Strain: 168 / BGSC1A1.
[7]	"Molecular basis for specificity of the extracytoplasmic thioredoxin ResA." Lewin A., Crow A., Oubrie A., Le Brun N.E. J. Biol. Chem. 281:35467-35477(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 37-179 WITH CYSTEINE MUTATIONS, CRYSTALLIZED AT HIGH PH. Strain: 168 / BGSC1A1.
[8]	"Mechanism of substrate specificity in Bacillus subtilis ResA, a thioredoxin-like protein involved in cytochrome c maturation." Colbert C.L., Wu Q., Erbel P.J.A., Gardner K.H., Deisenhofer J. Proc. Natl. Acad. Sci. U.S.A. 103:4410-4415(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 37-179, NMR. Strain: 168 / BGSC1A1.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L09228 Genomic DNA. Translation: AAA67494.1. Frameshift.
AL009126 Genomic DNA. Translation: CAB14247.2.

PIR

S45556.

RefSeq

NP_390196.2. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ST9	X-ray	1.50	A/B	37-179	[»]
1SU9	X-ray	1.95	A/B	37-179	[»]
2F9S	X-ray	1.40	A/B	37-179	[»]
2H19	X-ray	2.00	A/B	37-179	[»]
2H1A	X-ray	2.40	A/B	37-179	[»]
2H1B	X-ray	1.95	A/B/C/D	37-179	[»]
2H1D	X-ray	2.60	A/B	37-179	[»]
2H1G	X-ray	3.10	A/B	37-179	[»]
3C71	X-ray	1.90	A	37-179	[»]
3C73	X-ray	2.50	A/B	40-179	[»]

ProteinModelPortal

P35160.

SMR

P35160. Positions 38-175.

ModBase

Search...

Protein-protein interaction databases

STRING

224308.BSU23150.

Proteomic databases

PaxDb

P35160.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAB14247; CAB14247; BSU23150.

GeneID

938958.

KEGG

bsu:BSU23150.

PATRIC

18976447. VBIBacSub10457_2414.

Organism-specific databases

GenoList

BSU23150. [Micado]

Phylogenomic databases

eggNOG

COG0526.

HOGENOM

HOG000097217.

ProtClustDB

PRK03147.

Enzyme and pathway databases

BioCyc

BSUB:BSU23150-MONOMER.

UniPathway

UPA00555.

Family and domain databases

Gene3D

3.40.30.10. 1 hit.

HAMAP

MF_01319. ResA.

InterPro

IPR000866. AhpC/TSA.
IPR023555. Thiol-dS_OxRdtase_ResA.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
[Graphical view]

Pfam

PF00578. AhpC-TSA. 1 hit.
[Graphical view]

SUPFAM

SSF52833. Thiordxn-like_fd. 1 hit.

PROSITE

PS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P35160.

Entry information

Entry name

RESA_BACSU

Accession

Primary (citable) accession number: P35160

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	August 29, 2003
Last modified:	May 1, 2013
This is version 109 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program