TAMA_ECOLI
ID TAMA_ECOLI Reviewed; 577 AA.
AC P0ADE4; P39320; Q2M685;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Translocation and assembly module subunit TamA {ECO:0000303|PubMed:22466966};
DE AltName: Full=Autotransporter assembly factor TamA;
DE Flags: Precursor;
GN Name=tamA {ECO:0000303|PubMed:22466966}; Synonyms=yftM, ytfM;
GN OrderedLocusNames=b4220, JW4179;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP PROTEIN SEQUENCE OF 22-28, FUNCTION IN PROTEIN TRANSLOCATION, SUBCELLULAR
RP LOCATION, SUBUNIT, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=22466966; DOI=10.1038/nsmb.2261;
RA Selkrig J., Mosbahi K., Webb C.T., Belousoff M.J., Perry A.J., Wells T.J.,
RA Morris F., Leyton D.L., Totsika M., Phan M.D., Celik N., Kelly M.,
RA Oates C., Hartland E.L., Robins-Browne R.M., Ramarathinam S.H.,
RA Purcell A.W., Schembri M.A., Strugnell R.A., Henderson I.R., Walker D.,
RA Lithgow T.;
RT "Discovery of an archetypal protein transport system in bacterial outer
RT membranes.";
RL Nat. Struct. Mol. Biol. 19:506-510(2012).
RN [5]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=16522795; DOI=10.1110/ps.051889506;
RA Marani P., Wagner S., Baars L., Genevaux P., de Gier J.W., Nilsson I.,
RA Casadio R., von Heijne G.;
RT "New Escherichia coli outer membrane proteins identified through prediction
RT and experimental verification.";
RL Protein Sci. 15:884-889(2006).
RN [6]
RP SUBCELLULAR LOCATION, POSSIBLE TOPOLOGY, POSSIBLE CHANNEL-FORMING ABILITY,
RP AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / AG100;
RX PubMed=17214547; DOI=10.1515/bc.2007.004;
RA Stegmeier J.F., Gluck A., Sukumaran S., Mantele W., Andersen C.;
RT "Characterisation of YtfM, a second member of the Omp85 family in
RT Escherichia coli.";
RL Biol. Chem. 388:37-46(2007).
RN [7]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, AND TOPOLOGY.
RC STRAIN=K12 / BW25113;
RX PubMed=25341963; DOI=10.1038/ncomms6078;
RA Shen H.H., Leyton D.L., Shiota T., Belousoff M.J., Noinaj N., Lu J.,
RA Holt S.A., Tan K., Selkrig J., Webb C.T., Buchanan S.K., Martin L.L.,
RA Lithgow T.;
RT "Reconstitution of a nanomachine driving the assembly of proteins into
RT bacterial outer membranes.";
RL Nat. Commun. 5:5078-5078(2014).
RN [8] {ECO:0007744|PDB:4BZA, ECO:0007744|PDB:4C00}
RP X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 22-275, X-RAY CRYSTALLOGRAPHY
RP (2.25 ANGSTROMS) OF 22-577, AND TOPOLOGY.
RX PubMed=24056943; DOI=10.1038/nsmb.2689;
RA Gruss F., Zahringer F., Jakob R.P., Burmann B.M., Hiller S., Maier T.;
RT "The structural basis of autotransporter translocation by TamA.";
RL Nat. Struct. Mol. Biol. 20:1318-1320(2013).
RN [9] {ECO:0007744|PDB:2LY3}
RP STRUCTURE BY NMR OF 22-102, SUBUNIT, AND DOMAIN.
RX PubMed=26243377; DOI=10.1038/srep12905;
RA Selkrig J., Belousoff M.J., Headey S.J., Heinz E., Shiota T., Shen H.H.,
RA Beckham S.A., Bamert R.S., Phan M.D., Schembri M.A., Wilce M.C.,
RA Scanlon M.J., Strugnell R.A., Lithgow T.;
RT "Conserved features in TamA enable interaction with TamB to drive the
RT activity of the translocation and assembly module.";
RL Sci. Rep. 5:12905-12905(2015).
CC -!- FUNCTION: Part of the translocation and assembly module (TAM)
CC autotransporter assembly complex, which functions in translocation of
CC autotransporters across the outer membrane (PubMed:22466966,
CC PubMed:25341963). Allows substrate (Ag43, AC P39180) to initiate
CC penetration into the outer membrane; TamB is not necessary but may
CC regulate this activity (PubMed:25341963). Has anion selective channel-
CC forming ability, but the physiological relevance of this activity is
CC unclear (PubMed:22466966). {ECO:0000269|PubMed:22466966,
CC ECO:0000269|PubMed:25341963}.
CC -!- SUBUNIT: Interacts with TamB to form the translocation and assembly
CC module (TAM). {ECO:0000269|PubMed:22466966,
CC ECO:0000269|PubMed:24056943, ECO:0000269|PubMed:26243377}.
CC -!- INTERACTION:
CC P0ADE4; P39321: tamB; NbExp=3; IntAct=EBI-1114298, EBI-1117885;
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:16522795,
CC ECO:0000269|PubMed:17214547, ECO:0000269|PubMed:22466966,
CC ECO:0000269|PubMed:25341963}.
CC -!- DOMAIN: Contains 3 N-terminal periplasmic polypeptide transport-
CC associated (POTRA) domains and a C-terminal 16-stranded beta-barrel
CC transmembrane region (PubMed:24056943, PubMed:25341963). The 3 POTRA
CC domains seem to form a rigid body (unlike BamA where the 5 POTRA
CC domains are able to move independently) (PubMed:26243377). Upon
CC substrate binding (Ag43, AC P39180) the 3 POTRA domains move away from
CC the inner surface of the outer membrane by about 30 Angstroms, which
CC would deform either the outer membrane or TamB and may provide force to
CC reset TAM (PubMed:25341963). POTRA1 is required for interaction with
CC TamB (PubMed:26243377). Deletion of POTRA1 decreases Ag43 binding to
CC this protein, whereas deletion of POTRA1 and 2 obviates binding to Ag43
CC (PubMed:26243377). The beta-barrel is closed on the extracellular face
CC by loop 6 (residues 456-495), while the C-terminal beta-strand forms an
CC inward kink which may act as a gate for substrate access from the
CC periplasm. This kink weakens the beta-strand pair between the first and
CC last strands which may contribute to gating and substrate translocation
CC (PubMed:24056943). {ECO:0000269|PubMed:24056943,
CC ECO:0000269|PubMed:25341963, ECO:0000269|PubMed:26243377, ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Not essential, cells grow more slowly than wild-
CC type. No changes in permeability or outer membrane integrity. Loss of
CC localization of an exogenous protein, P1121 (ROD_p1121 of Citrobacter
CC rodentium), to outer membranes, loss of cell aggregation when adhesins
CC are over-expressed in a double tamA-tamB deletion mutant.
CC {ECO:0000269|PubMed:17214547, ECO:0000269|PubMed:22466966}.
CC -!- SIMILARITY: Belongs to the TamA family. {ECO:0000305}.
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DR EMBL; U14003; AAA97116.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77177.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78221.1; -; Genomic_DNA.
DR PIR; S56445; S56445.
DR RefSeq; NP_418641.1; NC_000913.3.
DR RefSeq; WP_001269327.1; NZ_SSUV01000014.1.
DR PDB; 2LY3; NMR; -; 1=22-102.
DR PDB; 4BZA; X-ray; 1.84 A; A=22-275.
DR PDB; 4C00; X-ray; 2.25 A; A=22-577.
DR PDBsum; 2LY3; -.
DR PDBsum; 4BZA; -.
DR PDBsum; 4C00; -.
DR AlphaFoldDB; P0ADE4; -.
DR BMRB; P0ADE4; -.
DR SMR; P0ADE4; -.
DR BioGRID; 4259308; 280.
DR ComplexPortal; CPX-5890; Translocation and assembly module complex.
DR DIP; DIP-51058N; -.
DR IntAct; P0ADE4; 7.
DR STRING; 511145.b4220; -.
DR TCDB; 1.B.33.2.4; the outer membrane protein insertion porin (bam complex) (ompip) family.
DR jPOST; P0ADE4; -.
DR PaxDb; P0ADE4; -.
DR PRIDE; P0ADE4; -.
DR EnsemblBacteria; AAC77177; AAC77177; b4220.
DR EnsemblBacteria; BAE78221; BAE78221; BAE78221.
DR GeneID; 66671861; -.
DR GeneID; 948733; -.
DR KEGG; ecj:JW4179; -.
DR KEGG; eco:b4220; -.
DR PATRIC; fig|1411691.4.peg.2480; -.
DR EchoBASE; EB2406; -.
DR eggNOG; COG0729; Bacteria.
DR HOGENOM; CLU_018618_1_0_6; -.
DR InParanoid; P0ADE4; -.
DR OMA; NTTMLLY; -.
DR PhylomeDB; P0ADE4; -.
DR BioCyc; EcoCyc:G7874-MON; -.
DR PRO; PR:P0ADE4; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IDA:EcoCyc.
DR GO; GO:0045203; C:integral component of cell outer membrane; IDA:EcoliWiki.
DR GO; GO:0005886; C:plasma membrane; IDA:ComplexPortal.
DR GO; GO:0097347; C:TAM protein secretion complex; IDA:EcoCyc.
DR GO; GO:0089705; P:protein localization to outer membrane; IDA:ComplexPortal.
DR GO; GO:0009306; P:protein secretion; IMP:EcoCyc.
DR InterPro; IPR000184; Bac_surfAg_D15.
DR InterPro; IPR010827; BamA/TamA_POTRA.
DR InterPro; IPR039910; D15-like.
DR InterPro; IPR034746; POTRA.
DR InterPro; IPR035243; TamA_POTRA_Dom_1.
DR PANTHER; PTHR12815; PTHR12815; 1.
DR Pfam; PF01103; Omp85; 1.
DR Pfam; PF07244; POTRA; 1.
DR Pfam; PF17243; POTRA_TamA_1; 1.
DR PROSITE; PS51779; POTRA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Direct protein sequencing; Membrane;
KW Protein transport; Reference proteome; Signal; Translocation;
KW Transmembrane; Transmembrane beta strand; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000305|PubMed:22466966"
FT CHAIN 22..577
FT /note="Translocation and assembly module subunit TamA"
FT /id="PRO_0000013946"
FT TOPO_DOM 22..264
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:24056943"
FT TRANSMEM 265..276
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:24056943"
FT TOPO_DOM 277..278
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:24056943"
FT TRANSMEM 279..288
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:24056943"
FT TOPO_DOM 289..296
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:24056943"
FT TRANSMEM 297..306
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:24056943"
FT TOPO_DOM 307..308
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:24056943"
FT TRANSMEM 309..317
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:24056943"
FT TOPO_DOM 318..326
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:24056943"
FT TRANSMEM 327..336
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:24056943"
FT TOPO_DOM 337..346
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:24056943"
FT TRANSMEM 347..356
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:24056943"
FT TOPO_DOM 357..360
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:24056943"
FT TRANSMEM 361..370
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:24056943"
FT TOPO_DOM 371..386
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:24056943"
FT TRANSMEM 387..395
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:24056943"
FT TOPO_DOM 396..405
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:24056943"
FT TRANSMEM 406..415
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:24056943"
FT TOPO_DOM 416..427
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:24056943"
FT TRANSMEM 428..437
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:24056943"
FT TOPO_DOM 438..443
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:24056943,
FT ECO:0000269|PubMed:25341963"
FT TRANSMEM 444..453
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:24056943"
FT TOPO_DOM 454..499
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:24056943"
FT TRANSMEM 500..508
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:24056943"
FT TOPO_DOM 509..513
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:24056943"
FT TRANSMEM 514..523
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:24056943"
FT TOPO_DOM 524..535
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:24056943"
FT TRANSMEM 536..545
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:24056943"
FT TOPO_DOM 546..548
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:24056943"
FT TRANSMEM 549..557
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:24056943"
FT TOPO_DOM 558..567
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:24056943"
FT TRANSMEM 568..577
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:24056943"
FT DOMAIN 187..263
FT /note="POTRA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01115"
FT REGION 22..106
FT /note="POTRA1, required for interaction with TamB"
FT /evidence="ECO:0000305|PubMed:26243377"
FT REGION 107..170
FT /note="POTRA2"
FT /evidence="ECO:0000305|PubMed:26243377"
FT REGION 171..250
FT /note="POTRA3"
FT /evidence="ECO:0000305|PubMed:26243377"
FT REGION 244..577
FT /note="Sufficient for outer membrane targeting"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:4BZA"
FT HELIX 34..43
FT /evidence="ECO:0007829|PDB:4BZA"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:4BZA"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:4BZA"
FT HELIX 58..71
FT /evidence="ECO:0007829|PDB:4BZA"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:4BZA"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:4BZA"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:4BZA"
FT STRAND 105..114
FT /evidence="ECO:0007829|PDB:4BZA"
FT HELIX 115..119
FT /evidence="ECO:0007829|PDB:4BZA"
FT HELIX 121..127
FT /evidence="ECO:0007829|PDB:4BZA"
FT HELIX 139..156
FT /evidence="ECO:0007829|PDB:4BZA"
FT STRAND 162..171
FT /evidence="ECO:0007829|PDB:4BZA"
FT TURN 172..175
FT /evidence="ECO:0007829|PDB:4BZA"
FT STRAND 176..184
FT /evidence="ECO:0007829|PDB:4BZA"
FT STRAND 190..198
FT /evidence="ECO:0007829|PDB:4BZA"
FT HELIX 203..207
FT /evidence="ECO:0007829|PDB:4BZA"
FT HELIX 220..232
FT /evidence="ECO:0007829|PDB:4BZA"
FT STRAND 236..243
FT /evidence="ECO:0007829|PDB:4BZA"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:4BZA"
FT TURN 248..251
FT /evidence="ECO:0007829|PDB:4BZA"
FT STRAND 253..262
FT /evidence="ECO:0007829|PDB:4BZA"
FT STRAND 267..275
FT /evidence="ECO:0007829|PDB:4C00"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:4C00"
FT STRAND 279..289
FT /evidence="ECO:0007829|PDB:4C00"
FT STRAND 297..318
FT /evidence="ECO:0007829|PDB:4C00"
FT TURN 323..325
FT /evidence="ECO:0007829|PDB:4C00"
FT STRAND 326..339
FT /evidence="ECO:0007829|PDB:4C00"
FT STRAND 342..356
FT /evidence="ECO:0007829|PDB:4C00"
FT STRAND 360..376
FT /evidence="ECO:0007829|PDB:4C00"
FT STRAND 379..402
FT /evidence="ECO:0007829|PDB:4C00"
FT STRAND 404..416
FT /evidence="ECO:0007829|PDB:4C00"
FT HELIX 418..420
FT /evidence="ECO:0007829|PDB:4C00"
FT STRAND 426..439
FT /evidence="ECO:0007829|PDB:4C00"
FT TURN 440..442
FT /evidence="ECO:0007829|PDB:4C00"
FT STRAND 443..457
FT /evidence="ECO:0007829|PDB:4C00"
FT HELIX 459..461
FT /evidence="ECO:0007829|PDB:4C00"
FT HELIX 464..466
FT /evidence="ECO:0007829|PDB:4C00"
FT TURN 473..475
FT /evidence="ECO:0007829|PDB:4C00"
FT STRAND 496..511
FT /evidence="ECO:0007829|PDB:4C00"
FT STRAND 514..527
FT /evidence="ECO:0007829|PDB:4C00"
FT STRAND 535..546
FT /evidence="ECO:0007829|PDB:4C00"
FT STRAND 549..560
FT /evidence="ECO:0007829|PDB:4C00"
FT STRAND 568..572
FT /evidence="ECO:0007829|PDB:4C00"
SQ SEQUENCE 577 AA; 64796 MW; 253D1D5BEA744D25 CRC64;
MRYIRQLCCV SLLCLSGSAV AANVRLQVEG LSGQLEKNVR AQLSTIESDE VTPDRRFRAR
VDDAIREGLK ALGYYQPTIE FDLRPPPKKG RQVLIAKVTP GVPVLIGGTD VVLRGGARTD
KDYLKLLDTR PAIGTVLNQG DYENFKKSLT SIALRKGYFD SEFTKAQLGI ALGLHKAFWD
IDYNSGERYR FGHVTFEGSQ IRDEYLQNLV PFKEGDEYES KDLAELNRRL SATGWFNSVV
VAPQFDKARE TKVLPLTGVV SPRTENTIET GVGYSTDVGP RVKATWKKPW MNSYGHSLTT
STSISAPEQT LDFSYKMPLL KNPLEQYYLV QGGFKRTDLN DTESDSTTLV ASRYWDLSSG
WQRAINLRWS LDHFTQGEIT NTTMLFYPGV MISRTRSRGG LMPTWGDSQR YSIDYSNTAW
GSDVDFSVFQ AQNVWIRTLY DRHRFVTRGT LGWIETGDFD KVPPDLRFFA GGDRSIRGYK
YKSIAPKYAN GDLKGASKLI TGSLEYQYNV TGKWWGAVFV DSGEAVSDIR RSDFKTGTGV
GVRWESPVGP IKLDFAVPVA DKDEHGLQFY IGLGPEL
