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Protein

Fe(3+)-binding periplasmic protein

Gene

fbpA

Organism
Serratia marcescens
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Part of the ABC transporter complex FbpABC (TC 3.A.1.10.1) involved in Fe3+ ions import. This protein specifically binds Fe3+ and is involved in its transmembrane transport (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi40 – 401IronBy similarity
Metal bindingi88 – 881IronBy similarity
Metal bindingi224 – 2241IronBy similarity
Metal bindingi225 – 2251IronBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Ion transport, Iron transport, Transport

Keywords - Ligandi

Iron, Metal-binding

Protein family/group databases

TCDBi3.A.1.10.1. the atp-binding cassette (abc) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Fe(3+)-binding periplasmic protein
Alternative name(s):
Iron(III)-binding periplasmic protein
Gene namesi
Name:fbpA
Synonyms:sfuA
OrganismiSerratia marcescens
Taxonomic identifieri615 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSerratia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence analysisAdd
BLAST
Chaini27 – 338312Fe(3+)-binding periplasmic proteinPRO_0000031704Add
BLAST

Interactioni

Subunit structurei

The complex is composed of two ATP-binding proteins (FbpC), two transmembrane proteins (FbpB) and a solute-binding protein (FbpA).Curated

Structurei

Secondary structure

1
338
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi33 – 375Combined sources
Helixi41 – 5515Combined sources
Beta strandi59 – 635Combined sources
Helixi66 – 7611Combined sources
Helixi77 – 793Combined sources
Beta strandi83 – 864Combined sources
Beta strandi88 – 903Combined sources
Helixi91 – 988Combined sources
Helixi107 – 1104Combined sources
Helixi115 – 1173Combined sources
Beta strandi123 – 13614Combined sources
Turni138 – 1403Combined sources
Helixi143 – 1453Combined sources
Helixi150 – 1545Combined sources
Helixi156 – 1583Combined sources
Beta strandi161 – 1644Combined sources
Helixi169 – 19729Combined sources
Beta strandi198 – 2003Combined sources
Helixi204 – 2129Combined sources
Beta strandi215 – 2228Combined sources
Helixi224 – 2318Combined sources
Turni235 – 2395Combined sources
Beta strandi241 – 2433Combined sources
Helixi250 – 2523Combined sources
Beta strandi254 – 2629Combined sources
Helixi268 – 27912Combined sources
Helixi281 – 2899Combined sources
Beta strandi290 – 2923Combined sources
Helixi310 – 3134Combined sources
Helixi320 – 3223Combined sources
Helixi325 – 33410Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XVYX-ray1.74A30-338[»]
ProteinModelPortaliP21408.
SMRiP21408. Positions 32-338.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21408.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

InterProiIPR026045. Ferric-bd.
IPR006061. SBP_1_CS.
[Graphical view]
PIRSFiPIRSF002825. CfbpA. 1 hit.
PROSITEiPS01037. SBP_BACTERIAL_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P21408-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLRISSLGP VALLASSMML AFGAQAASAD QGIVIYNAQH ENLVKSWVDG
60 70 80 90 100
FTKDTGIKVT LRNGGDSELG NQLVQEGSAS PADVFLTENS PAMVLVDNAK
110 120 130 140 150
LFAPLDAATL AQVEPQYRPS HGRWIGIAAR STVFVYNPAK LSDAQLPKSL
160 170 180 190 200
LDLAKPEWKG RWAASPSGAD FQAIVSALLE LKGEKATLAW LKAMKTNFTA
210 220 230 240 250
YKGNSTVMKA VNAGQVDSGV IYHYYPFVDG AKTGENSNNI KLYYFKHQDP
260 270 280 290 300
GAFVSISGGG VLASSKHQQQ AQAFIKWITG KQGQEILRTN NAFEYAVGVG
310 320 330
AASNPKLVPL KDLDAPKVDA AQLNSKKVVE LMTEAGLL
Length:338
Mass (Da):36,157
Last modified:May 1, 1991 - v1
Checksum:iDD5FAA452301A716
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M33815 Genomic DNA. Translation: AAA26573.1.
PIRiA35108. QRSEUA.
RefSeqiWP_016927639.1. NZ_KN050642.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M33815 Genomic DNA. Translation: AAA26573.1.
PIRiA35108. QRSEUA.
RefSeqiWP_016927639.1. NZ_KN050642.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XVYX-ray1.74A30-338[»]
ProteinModelPortaliP21408.
SMRiP21408. Positions 32-338.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

TCDBi3.A.1.10.1. the atp-binding cassette (abc) superfamily.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP21408.

Family and domain databases

InterProiIPR026045. Ferric-bd.
IPR006061. SBP_1_CS.
[Graphical view]
PIRSFiPIRSF002825. CfbpA. 1 hit.
PROSITEiPS01037. SBP_BACTERIAL_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Nucleotide sequences of the sfuA, sfuB, and sfuC genes of Serratia marcescens suggest a periplasmic-binding-protein-dependent iron transport mechanism."
    Angerer A., Gaisser S., Braun V.
    J. Bacteriol. 172:572-578(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiFBPA_SERMA
AccessioniPrimary (citable) accession number: P21408
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: October 14, 2015
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.