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Protein

Translocation and assembly module subunit TamA

Gene

tamA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Part of the translocation and assembly module (TAM) autotransporter assembly complex, which functions in translocation of autotransporters across the outer membrane (PubMed:22466966, PubMed:25341963). Allows substrate (Ag43, AC P39180) to initiate penetration into the outer membrane; TamB is not necessary but may regulate this activity (PubMed:25341963). Has anion selective channel-forming ability, but the physiological relevance of this activity is unclear (PubMed:22466966).2 Publications

GO - Biological processi

  • protein secretion Source: EcoCyc

Keywordsi

Biological processProtein transport, Translocation, Transport

Enzyme and pathway databases

BioCyciEcoCyc:G7874-MONOMER.

Protein family/group databases

TCDBi1.B.33.2.4. the outer membrane protein insertion porin (bam complex) (ompip) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Translocation and assembly module subunit TamA1 Publication
Alternative name(s):
Autotransporter assembly factor TamA
Gene namesi
Name:tamA1 Publication
Synonyms:yftM, ytfM
Ordered Locus Names:b4220, JW4179
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12513. tamA.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini22 – 264Periplasmic, turn 11 PublicationAdd BLAST243
Transmembranei265 – 276Beta stranded1 PublicationAdd BLAST12
Topological domaini277 – 278Extracellular, loop 11 Publication2
Transmembranei279 – 288Beta stranded1 Publication10
Topological domaini289 – 296Periplasmic, turn 21 Publication8
Transmembranei297 – 306Beta stranded1 Publication10
Topological domaini307 – 308Extracellular, loop 21 Publication2
Transmembranei309 – 317Beta stranded1 Publication9
Topological domaini318 – 326Periplasmic, turn 31 Publication9
Transmembranei327 – 336Beta stranded1 Publication10
Topological domaini337 – 346Extracellular, loop 31 Publication10
Transmembranei347 – 356Beta stranded1 Publication10
Topological domaini357 – 360Periplasmic, turn 41 Publication4
Transmembranei361 – 370Beta stranded1 Publication10
Topological domaini371 – 386Extracellular, loop 41 PublicationAdd BLAST16
Transmembranei387 – 395Beta stranded1 Publication9
Topological domaini396 – 405Periplasmic, turn 51 Publication10
Transmembranei406 – 415Beta stranded1 Publication10
Topological domaini416 – 427Extracellular, loop 51 PublicationAdd BLAST12
Transmembranei428 – 437Beta stranded1 Publication10
Topological domaini438 – 443Periplasmic, turn 62 Publications6
Transmembranei444 – 453Beta stranded1 Publication10
Topological domaini454 – 499Extracellular, loop 61 PublicationAdd BLAST46
Transmembranei500 – 508Beta stranded1 Publication9
Topological domaini509 – 513Periplasmic, turn 71 Publication5
Transmembranei514 – 523Beta stranded1 Publication10
Topological domaini524 – 535Extracellular, loop 71 PublicationAdd BLAST12
Transmembranei536 – 545Beta stranded1 Publication10
Topological domaini546 – 548Periplasmic, turn 81 Publication3
Transmembranei549 – 557Beta stranded1 Publication9
Topological domaini558 – 567Extracellular, loop 81 Publication10
Transmembranei568 – 577Beta stranded1 Publication10

GO - Cellular componenti

  • cell outer membrane Source: EcoCyc
  • integral component of cell outer membrane Source: EcoliWiki
  • TAM protein secretion complex Source: EcoCyc

Keywords - Cellular componenti

Cell outer membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Not essential, cells grow more slowly than wild-type. No changes in permeability or outer membrane integrity. Loss of localization of an exogenous protein, P1121 (ROD_p1121 of Citrobacter rodentium), to outer membranes, loss of cell aggregation when adhesins are over-expressed in a double tamA-tamB deletion mutant.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 211 PublicationAdd BLAST21
ChainiPRO_000001394622 – 577Translocation and assembly module subunit TamAAdd BLAST556

Proteomic databases

PaxDbiP0ADE4.
PRIDEiP0ADE4.

Interactioni

Subunit structurei

Interacts with TamB to form the translocation and assembly module (TAM).3 Publications

Protein-protein interaction databases

BioGridi4259308. 242 interactors.
DIPiDIP-51058N.
IntActiP0ADE4. 6 interactors.
STRINGi511145.b4220.

Structurei

Secondary structure

1577
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi26 – 30Combined sources5
Helixi34 – 43Combined sources10
Beta strandi49 – 51Combined sources3
Beta strandi54 – 57Combined sources4
Helixi58 – 71Combined sources14
Beta strandi74 – 76Combined sources3
Beta strandi78 – 80Combined sources3
Beta strandi94 – 99Combined sources6
Beta strandi105 – 114Combined sources10
Helixi115 – 119Combined sources5
Helixi121 – 127Combined sources7
Helixi139 – 156Combined sources18
Beta strandi162 – 171Combined sources10
Turni172 – 175Combined sources4
Beta strandi176 – 184Combined sources9
Beta strandi190 – 198Combined sources9
Helixi203 – 207Combined sources5
Helixi220 – 232Combined sources13
Beta strandi236 – 243Combined sources8
Helixi245 – 247Combined sources3
Turni248 – 251Combined sources4
Beta strandi253 – 262Combined sources10
Beta strandi267 – 275Combined sources9
Turni276 – 278Combined sources3
Beta strandi279 – 289Combined sources11
Beta strandi297 – 318Combined sources22
Turni323 – 325Combined sources3
Beta strandi326 – 339Combined sources14
Beta strandi342 – 356Combined sources15
Beta strandi360 – 376Combined sources17
Beta strandi379 – 402Combined sources24
Beta strandi404 – 416Combined sources13
Helixi418 – 420Combined sources3
Beta strandi426 – 439Combined sources14
Turni440 – 442Combined sources3
Beta strandi443 – 457Combined sources15
Helixi459 – 461Combined sources3
Helixi464 – 466Combined sources3
Turni473 – 475Combined sources3
Beta strandi496 – 511Combined sources16
Beta strandi514 – 527Combined sources14
Beta strandi535 – 546Combined sources12
Beta strandi549 – 560Combined sources12
Beta strandi568 – 572Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2LY3NMR-122-102[»]
4BZAX-ray1.84A22-275[»]
4C00X-ray2.25A22-577[»]
ProteinModelPortaliP0ADE4.
SMRiP0ADE4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini187 – 263POTRAPROSITE-ProRule annotationAdd BLAST77

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni22 – 106POTRA1, required for interaction with TamB1 PublicationAdd BLAST85
Regioni107 – 170POTRA21 PublicationAdd BLAST64
Regioni171 – 250POTRA31 PublicationAdd BLAST80
Regioni244 – 577Sufficient for outer membrane targetingAdd BLAST334

Domaini

Contains 3 N-terminal periplasmic polypeptide transport-associated (POTRA) domains and a C-terminal 16-stranded beta-barrel transmembrane region (PubMed:24056943, PubMed:25341963). The 3 POTRA domains seem to form a rigid body (unlike BamA where the 5 POTRA domains are able to move independently) (PubMed:26243377). Upon substrate binding (Ag43, AC P39180) the 3 POTRA domains move away from the inner surface of the outer membrane by about 30 Angstroms, which would deform either the outer membrane or TamB and may provide force to reset TAM (PubMed:25341963). POTRA1 is required for interaction with TamB (PubMed:26243377). Deletion of POTRA1 decreases Ag43 binding to this protein, whereas deletion of POTRA1 and 2 obviates binding to Ag43 (PubMed:26243377). The beta-barrel is closed on the extracellular face by loop 6 (residues 456-495), while the C-terminal beta-strand forms an inward kink which may act as a gate for substrate access from the periplasm. This kink weakens the beta-strand pair between the first and last strands which may contribute to gating and substrate translocation (PubMed:24056943).Curated3 Publications

Sequence similaritiesi

Belongs to the TamA family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane beta strand

Phylogenomic databases

eggNOGiENOG4105CFU. Bacteria.
COG0729. LUCA.
HOGENOMiHOG000275353.
InParanoidiP0ADE4.
KOiK07278.
OMAiWDSSSGW.
PhylomeDBiP0ADE4.

Family and domain databases

InterProiView protein in InterPro
IPR000184. Bac_surfAg_D15.
IPR010827. BamA/TamA_POTRA.
IPR034746. POTRA.
PfamiView protein in Pfam
PF01103. Bac_surface_Ag. 1 hit.
PF07244. POTRA. 1 hit.
PROSITEiView protein in PROSITE
PS51779. POTRA. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P0ADE4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRYIRQLCCV SLLCLSGSAV AANVRLQVEG LSGQLEKNVR AQLSTIESDE
60 70 80 90 100
VTPDRRFRAR VDDAIREGLK ALGYYQPTIE FDLRPPPKKG RQVLIAKVTP
110 120 130 140 150
GVPVLIGGTD VVLRGGARTD KDYLKLLDTR PAIGTVLNQG DYENFKKSLT
160 170 180 190 200
SIALRKGYFD SEFTKAQLGI ALGLHKAFWD IDYNSGERYR FGHVTFEGSQ
210 220 230 240 250
IRDEYLQNLV PFKEGDEYES KDLAELNRRL SATGWFNSVV VAPQFDKARE
260 270 280 290 300
TKVLPLTGVV SPRTENTIET GVGYSTDVGP RVKATWKKPW MNSYGHSLTT
310 320 330 340 350
STSISAPEQT LDFSYKMPLL KNPLEQYYLV QGGFKRTDLN DTESDSTTLV
360 370 380 390 400
ASRYWDLSSG WQRAINLRWS LDHFTQGEIT NTTMLFYPGV MISRTRSRGG
410 420 430 440 450
LMPTWGDSQR YSIDYSNTAW GSDVDFSVFQ AQNVWIRTLY DRHRFVTRGT
460 470 480 490 500
LGWIETGDFD KVPPDLRFFA GGDRSIRGYK YKSIAPKYAN GDLKGASKLI
510 520 530 540 550
TGSLEYQYNV TGKWWGAVFV DSGEAVSDIR RSDFKTGTGV GVRWESPVGP
560 570
IKLDFAVPVA DKDEHGLQFY IGLGPEL
Length:577
Mass (Da):64,796
Last modified:December 6, 2005 - v1
Checksum:i253D1D5BEA744D25
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14003 Genomic DNA. Translation: AAA97116.1.
U00096 Genomic DNA. Translation: AAC77177.1.
AP009048 Genomic DNA. Translation: BAE78221.1.
PIRiS56445.
RefSeqiNP_418641.1. NC_000913.3.
WP_001269327.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77177; AAC77177; b4220.
BAE78221; BAE78221; BAE78221.
GeneIDi948733.
KEGGiecj:JW4179.
eco:b4220.
PATRICi32124017. VBIEscCol129921_4353.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14003 Genomic DNA. Translation: AAA97116.1.
U00096 Genomic DNA. Translation: AAC77177.1.
AP009048 Genomic DNA. Translation: BAE78221.1.
PIRiS56445.
RefSeqiNP_418641.1. NC_000913.3.
WP_001269327.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2LY3NMR-122-102[»]
4BZAX-ray1.84A22-275[»]
4C00X-ray2.25A22-577[»]
ProteinModelPortaliP0ADE4.
SMRiP0ADE4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259308. 242 interactors.
DIPiDIP-51058N.
IntActiP0ADE4. 6 interactors.
STRINGi511145.b4220.

Protein family/group databases

TCDBi1.B.33.2.4. the outer membrane protein insertion porin (bam complex) (ompip) family.

Proteomic databases

PaxDbiP0ADE4.
PRIDEiP0ADE4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77177; AAC77177; b4220.
BAE78221; BAE78221; BAE78221.
GeneIDi948733.
KEGGiecj:JW4179.
eco:b4220.
PATRICi32124017. VBIEscCol129921_4353.

Organism-specific databases

EchoBASEiEB2406.
EcoGeneiEG12513. tamA.

Phylogenomic databases

eggNOGiENOG4105CFU. Bacteria.
COG0729. LUCA.
HOGENOMiHOG000275353.
InParanoidiP0ADE4.
KOiK07278.
OMAiWDSSSGW.
PhylomeDBiP0ADE4.

Enzyme and pathway databases

BioCyciEcoCyc:G7874-MONOMER.

Miscellaneous databases

PROiPR:P0ADE4.

Family and domain databases

InterProiView protein in InterPro
IPR000184. Bac_surfAg_D15.
IPR010827. BamA/TamA_POTRA.
IPR034746. POTRA.
PfamiView protein in Pfam
PF01103. Bac_surface_Ag. 1 hit.
PF07244. POTRA. 1 hit.
PROSITEiView protein in PROSITE
PS51779. POTRA. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiTAMA_ECOLI
AccessioniPrimary (citable) accession number: P0ADE4
Secondary accession number(s): P39320, Q2M685
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: May 10, 2017
This is version 93 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.