P45038 (DSBE_HAEIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Thiol:disulfide interchange protein DsbE

Alternative name(s):
Cytochrome c biogenesis protein CcmG

Gene names

Name:	dsbE
Synonyms:	ccmG
Ordered Locus Names:	HI_1095

Organism

Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP]

Taxonomic identifier

71421 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus › Haemophilus influenzae

Protein attributes

Sequence length	181 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Involved in disulfide bond formation. Catalyzes a late, reductive step in the assembly of periplasmic c-type cytochromes, probably the reduction of disulfide bonds of the apocytochrome c to allow covalent linkage with the heme. Possible subunit of a heme lyase By similarity.
Subcellular location	Cell inner membrane; Single-pass membrane protein; Periplasmic side By similarity.
Sequence similarities	Belongs to the thioredoxin family. DsbE subfamily. Contains 1 thioredoxin domain.

Ontologies

Keywords
Biological process	Cytochrome c-type biogenesis
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Redox-active center Transmembrane Transmembrane helix
PTM	Disulfide bond
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro cytochrome complex assembly Inferred from electronic annotation. Source: UniProtKB-KW oxidation-reduction process Inferred from electronic annotation. Source: GOC
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW outer membrane-bounded periplasmic space Inferred from electronic annotation. Source: InterPro plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	disulfide oxidoreductase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 181	181	Thiol:disulfide interchange protein DsbE		PRO_0000201295
Regions
	Topological domain	1 – 4	4	Cytoplasmic Potential
	Transmembrane	5 – 23	19	Helical; Potential
	Topological domain	24 – 181	158	Periplasmic Potential
	Domain	38 – 175	138	Thioredoxin
Amino acid modifications
	Disulfide bond	78 ↔ 81		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	P45038 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 4B334B444179EF24	FASTA	181	20,535
	10 20 30 40 50 60 MKKKLLVPLI LFLSITIAFL VQLKRNAQGE DIKALESALV GKPVPAKNLT ELFENKTYTN 70 80 90 100 110 120 ELFQQGEPVL LNVWATWCPT CYAEHQYLNK LAKEGVRIIG LDYKDESPKA MKWLKDLGNP 130 140 150 160 170 180 YQVVLKDEKG SFGLDLGVYG APETFIVDGK GVIHYRYAGD VNEKVWTQTL KPIYDKLSEQ Q

References

[1]

"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C. Science 269:496-512(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L42023 Genomic DNA. Translation: AAC22752.1.
PIR	B64167.
RefSeq	NP_439252.1. NC_000907.1.
3D structure databases
ProteinModelPortal	P45038.
SMR	P45038. Positions 54-181.
ModBase	Search...
Protein-protein interaction databases
STRING	71421.HI1095.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC22752; AAC22752; HI_1095.
GeneID	950067.
KEGG	hin:HI1095.
PATRIC	20190855. VBIHaeInf48452_1140.
Phylogenomic databases
eggNOG	COG0526.
KO	K02199.
OMA	GNPYQVI.
ProtClustDB	CLSK869931.
Family and domain databases
Gene3D	3.40.30.10. 1 hit.
InterPro	IPR004799. Periplasmic_diS_OxRdtase_DsbE. IPR013740. Redoxin. IPR012336. Thioredoxin-like_fold. IPR017937. Thioredoxin_CS. [Graphical view]
Pfam	PF08534. Redoxin. 1 hit. [Graphical view]
SUPFAM	SSF52833. Thiordxn-like_fd. 1 hit.
TIGRFAMs	TIGR00385. dsbE. 1 hit.
PROSITE	PS00194. THIOREDOXIN_1. 1 hit. PS51352. THIOREDOXIN_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DSBE_HAEIN

Accession

Primary (citable) accession number: P45038

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 1, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program