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Protein

Filamentous hemagglutinin transporter protein FhaC

Gene

fhaC

Organism
Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Member of a two partner secretion pathway (TPS) in which it mediates the secretion of filamentous hemagglutinin FHA (fhaB).2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Porin

Keywords - Biological processi

Ion transport, Protein transport, Transport

Enzyme and pathway databases

BioCyciBPER257313:BP1884-MONOMER.

Protein family/group databases

TCDBi1.B.20.1.6. the two-partner secretion (tps) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Filamentous hemagglutinin transporter protein FhaC
Alternative name(s):
TpsB transporter
Gene namesi
Name:fhaC
Ordered Locus Names:BP1884
OrganismiBordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
Taxonomic identifieri257313 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella
Proteomesi
  • UP000002676 Componenti: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei242 – 2487Beta stranded1 Publication
Transmembranei261 – 2699Beta stranded1 Publication
Transmembranei277 – 2859Beta stranded1 Publication
Transmembranei294 – 30613Beta stranded1 PublicationAdd
BLAST
Transmembranei309 – 32113Beta stranded1 PublicationAdd
BLAST
Transmembranei334 – 34916Beta stranded1 PublicationAdd
BLAST
Transmembranei354 – 37017Beta stranded1 PublicationAdd
BLAST
Transmembranei378 – 39518Beta stranded1 PublicationAdd
BLAST
Transmembranei399 – 40911Beta stranded1 PublicationAdd
BLAST
Transmembranei431 – 44414Beta stranded1 PublicationAdd
BLAST
Transmembranei449 – 46012Beta stranded1 PublicationAdd
BLAST
Transmembranei500 – 51011Beta stranded1 PublicationAdd
BLAST
Transmembranei516 – 52712Beta stranded1 PublicationAdd
BLAST
Transmembranei537 – 54711Beta stranded1 PublicationAdd
BLAST
Transmembranei552 – 56211Beta stranded1 PublicationAdd
BLAST
Transmembranei575 – 58410Beta stranded1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell outer membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3030Sequence analysisAdd
BLAST
Chaini31 – 584554Filamentous hemagglutinin transporter protein FhaCPRO_0000018666Add
BLAST

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

IntActiP35077. 1 interaction.
MINTiMINT-7996278.
STRINGi257313.BP1884.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi36 – 6126Combined sources
Beta strandi85 – 873Combined sources
Beta strandi92 – 976Combined sources
Helixi99 – 1013Combined sources
Helixi108 – 1114Combined sources
Helixi112 – 1143Combined sources
Beta strandi115 – 1173Combined sources
Helixi121 – 13717Combined sources
Beta strandi144 – 15310Combined sources
Beta strandi156 – 1627Combined sources
Beta strandi165 – 1717Combined sources
Helixi179 – 18810Combined sources
Helixi199 – 20911Combined sources
Beta strandi211 – 22212Combined sources
Beta strandi228 – 23710Combined sources
Beta strandi242 – 2487Combined sources
Beta strandi257 – 26913Combined sources
Beta strandi271 – 2755Combined sources
Beta strandi277 – 28913Combined sources
Turni290 – 2923Combined sources
Beta strandi294 – 30613Combined sources
Beta strandi309 – 32315Combined sources
Beta strandi332 – 35019Combined sources
Beta strandi352 – 37524Combined sources
Beta strandi377 – 39620Combined sources
Beta strandi399 – 40911Combined sources
Beta strandi431 – 44717Combined sources
Beta strandi449 – 46012Combined sources
Helixi467 – 4693Combined sources
Beta strandi470 – 4734Combined sources
Beta strandi478 – 4814Combined sources
Turni484 – 4863Combined sources
Beta strandi488 – 50114Combined sources
Beta strandi504 – 5063Combined sources
Beta strandi513 – 52715Combined sources
Beta strandi530 – 5323Combined sources
Beta strandi535 – 54915Combined sources
Beta strandi552 – 56110Combined sources
Beta strandi575 – 58410Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NJTX-ray3.50A34-584[»]
4QKYX-ray2.90A31-584[»]
4QL0X-ray2.50A31-584[»]
ProteinModelPortaliP35077.
SMRiP35077. Positions 33-584.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35077.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini89 – 16476POTRAPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni38 – 5821Alpha helix H1, not required for FHA secretion1 PublicationAdd
BLAST
Regioni89 – 16476POTRA 1; required for FHA secretion but not channel formationSequence analysis1 PublicationAdd
BLAST
Regioni165 – 23874POTRA 2; required for FHA secretion but not channel formationSequence analysis1 PublicationAdd
BLAST
Regioni462 – 50443Loop L6, required for FHA secretion and possibly for channel stability1 PublicationAdd
BLAST

Domaini

In the crystal structure alpha helix H1 passes through the middle of the pore with its C-terminus in the periplasm and loop L6 also blocks the channel. Both of the POTRA domains are periplasmic; POTRA stands for polypeptide-transport associated.1 Publication

Sequence similaritiesi

Contains 1 POTRA domain.PROSITE-ProRule annotation
Contains 2 POTRA domains.

Keywords - Domaini

Signal, Transmembrane, Transmembrane beta strand

Phylogenomic databases

eggNOGiENOG4108YH7. Bacteria.
COG2831. LUCA.
HOGENOMiHOG000112585.
KOiK07326.
OMAiQYSRDPL.
OrthoDBiEOG6GBM6J.

Family and domain databases

InterProiIPR005565. Hemolysn_activator_HlyB.
IPR013686. Polypept-transport_assoc_ShlB.
IPR027282. TPS.
[Graphical view]
PfamiPF08479. POTRA_2. 1 hit.
PF03865. ShlB. 1 hit.
[Graphical view]
PIRSFiPIRSF029745. FhaC. 1 hit.
PROSITEiPS51779. POTRA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P35077-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDATNRFRP GLVGRALVRA GLLFAVAACA QAQLLPGARD LNRIDDRQRK
60 70 80 90 100
EQLQRDIERA LTRPPVELNP QSEAAAPARK PDATSGHTVT VHAVDLDFGV
110 120 130 140 150
EGRLFDPAPL VQDYLNRPLD NEQLFLLVKA LSAALYDRGY ATSIVTFVPP
160 170 180 190 200
GVVDGVLKLK VEWGRIKGWL IDGKPLEGTR DRMMVFSAMP GWQDKVLNVF
210 220 230 240 250
DIDQAIYNIN NGGKTGNITI VPADEYGYSY LDLQLQRRAL PRVSLGMDNS
260 270 280 290 300
GPGTPENGRY KYNASVTAND LLGLNDTLGL YIGNRYYRDA GHDAERNYDL
310 320 330 340 350
MYSVPLGRTR LDLQTGYSTY RNLLKTRYGQ YQSAGNSRSF GLKATRLLYR
360 370 380 390 400
DTRSQFSVYG GLKLRQNKNY LAGTRLDVSS KHYSDVTVGM QYSTQRGANA
410 420 430 440 450
YFGDLSFTRG VGVNNGKYAA YDERGPQGNV SRFNGSLAWT RYMALAGQPI
460 470 480 490 500
QWASQLGFQY SRQQLLNSYQ ITVGDEYTVR GYNLRTSQSG DSGVYLSNTL
510 520 530 540 550
TVPVQFSLLG KQASVAPFVG ADVGALKSNH PDARTIRMAG LAAGVRFDLP
560 570 580
YARMSFTYSK PVGAQPGGAP RAPVWLYINA GLSF
Length:584
Mass (Da):64,446
Last modified:February 1, 1994 - v1
Checksum:i8E625B2C07702178
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64876 Genomic DNA. Translation: CAA46092.1.
BX640416 Genomic DNA. Translation: CAE42167.1.
PIRiS41526.
RefSeqiNP_880575.1. NC_002929.2.
WP_010930614.1. NC_002929.2.

Genome annotation databases

EnsemblBacteriaiCAE42167; CAE42167; BP1884.
GeneIDi2667436.
KEGGibpe:BP1884.
PATRICi21157054. VBIBorPer7866_2022.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64876 Genomic DNA. Translation: CAA46092.1.
BX640416 Genomic DNA. Translation: CAE42167.1.
PIRiS41526.
RefSeqiNP_880575.1. NC_002929.2.
WP_010930614.1. NC_002929.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NJTX-ray3.50A34-584[»]
4QKYX-ray2.90A31-584[»]
4QL0X-ray2.50A31-584[»]
ProteinModelPortaliP35077.
SMRiP35077. Positions 33-584.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP35077. 1 interaction.
MINTiMINT-7996278.
STRINGi257313.BP1884.

Protein family/group databases

TCDBi1.B.20.1.6. the two-partner secretion (tps) family.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAE42167; CAE42167; BP1884.
GeneIDi2667436.
KEGGibpe:BP1884.
PATRICi21157054. VBIBorPer7866_2022.

Phylogenomic databases

eggNOGiENOG4108YH7. Bacteria.
COG2831. LUCA.
HOGENOMiHOG000112585.
KOiK07326.
OMAiQYSRDPL.
OrthoDBiEOG6GBM6J.

Enzyme and pathway databases

BioCyciBPER257313:BP1884-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP35077.

Family and domain databases

InterProiIPR005565. Hemolysn_activator_HlyB.
IPR013686. Polypept-transport_assoc_ShlB.
IPR027282. TPS.
[Graphical view]
PfamiPF08479. POTRA_2. 1 hit.
PF03865. ShlB. 1 hit.
[Graphical view]
PIRSFiPIRSF029745. FhaC. 1 hit.
PROSITEiPS51779. POTRA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Willems R.J.L.
    Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Wellcome 28.
  2. "Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica."
    Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S.
    , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J.
    Nat. Genet. 35:32-40(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Tohama I / ATCC BAA-589 / NCTC 13251.
  3. "Secretion signal of the filamentous haemagglutinin, a model two-partner secretion substrate."
    Hodak H., Clantin B., Willery E., Villeret V., Locht C., Jacob-Dubuisson F.
    Mol. Microbiol. 61:368-382(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
    Strain: Tohama I / BPSM.
  4. "Structure of the membrane protein FhaC: a member of the Omp85-TpsB transporter superfamily."
    Clantin B., Delattre A.S., Rucktooa P., Saint N., Meli A.C., Locht C., Jacob-Dubuisson F., Villeret V.
    Science 317:957-961(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 31-584, FUNCTION, SUBUNIT, DOMAIN, MUTAGENESIS.
    Strain: Tohama I / BPSM.

Entry informationi

Entry nameiFHAC_BORPE
AccessioniPrimary (citable) accession number: P35077
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: December 9, 2015
This is version 95 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, Complete proteome, Reference proteome

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.