TAMB_ECOLI
ID TAMB_ECOLI Reviewed; 1259 AA.
AC P39321; P39322; P76802; Q2M684;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Translocation and assembly module subunit TamB {ECO:0000303|PubMed:22466966};
DE AltName: Full=Autotransporter assembly factor TamB;
GN Name=tamB {ECO:0000303|PubMed:22466966}; Synonyms=ytfN, ytfO;
GN OrderedLocusNames=b4221, JW4180;
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], AND SEQUENCE REVISION.
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 1-6, FUNCTION IN PROTEIN TRANSLOCATION, SUBCELLULAR
RP LOCATION, SUBUNIT, FORMYLATION AT MET-1, 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 FUNCTION, SUBUNIT, 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 [6]
RP SUBUNIT.
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). In
CC reconstituted TAM this subunit (Ag43, AC P39180) is not necessary for
CC substrate penetration in the outer membrane. Substrate binding to TamA
CC moves its POTRA domains about 30 Angstroms into the periplasm, which
CC would deform either the outer membrane or TamB and may provide force to
CC reset TAM (PubMed:25341963). {ECO:0000269|PubMed:22466966,
CC ECO:0000269|PubMed:25341963}.
CC -!- SUBUNIT: Interacts with TamA to form the translocation and assembly
CC module (TAM). {ECO:0000269|PubMed:22466966,
CC ECO:0000269|PubMed:25341963, ECO:0000269|PubMed:26243377}.
CC -!- INTERACTION:
CC P39321; P0ADE4: tamA; NbExp=3; IntAct=EBI-1117885, EBI-1114298;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:22466966}; Single-pass membrane protein
CC {ECO:0000305|PubMed:22466966}.
CC -!- DOMAIN: The periplasmic domain is elongated (up to 160 Angstroms long)
CC and forms contacts with the N-terminal POTRA domains of TamA
CC (PubMed:25341963). {ECO:0000269|PubMed:25341963}.
CC -!- DISRUPTION PHENOTYPE: Loss of localization of an exogenous protein,
CC P1121 (ROD_p1121 of Citrobacter rodentium), to outer membranes, loss of
CC cell aggregation when adhesins are over-expressed in a double tamA-tamB
CC deletion mutant. {ECO:0000269|PubMed:22466966}.
CC -!- SIMILARITY: Belongs to the TamB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA97118.1; Type=Frameshift; Note=Produces two separate ORFs.; Evidence={ECO:0000305};
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DR EMBL; U14003; AAA97117.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U14003; AAA97118.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00096; AAC77178.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78222.1; -; Genomic_DNA.
DR PIR; H65233; H65233.
DR RefSeq; NP_418642.1; NC_000913.3.
DR RefSeq; WP_000060911.1; NZ_CP047127.1.
DR PDB; 5VTG; X-ray; 1.86 A; A/B=963-1138.
DR PDBsum; 5VTG; -.
DR AlphaFoldDB; P39321; -.
DR SMR; P39321; -.
DR BioGRID; 4259309; 404.
DR ComplexPortal; CPX-5890; Translocation and assembly module complex.
DR DIP; DIP-12942N; -.
DR IntAct; P39321; 7.
DR STRING; 511145.b4221; -.
DR TCDB; 9.B.22.1.2; the leukotoxin secretion morphogenesis protein c (morc) family.
DR jPOST; P39321; -.
DR PaxDb; P39321; -.
DR PRIDE; P39321; -.
DR EnsemblBacteria; AAC77178; AAC77178; b4221.
DR EnsemblBacteria; BAE78222; BAE78222; BAE78222.
DR GeneID; 948742; -.
DR KEGG; ecj:JW4180; -.
DR KEGG; eco:b4221; -.
DR PATRIC; fig|1411691.4.peg.2479; -.
DR EchoBASE; EB2407; -.
DR eggNOG; COG2911; Bacteria.
DR HOGENOM; CLU_002338_0_1_6; -.
DR InParanoid; P39321; -.
DR OMA; NTAKQWP; -.
DR PhylomeDB; P39321; -.
DR BioCyc; EcoCyc:G7875-MON; -.
DR PRO; PR:P39321; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IDA:ComplexPortal.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
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; IPR007452; TamB.
DR Pfam; PF04357; TamB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane;
KW Direct protein sequencing; Formylation; Membrane; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..1259
FT /note="Translocation and assembly module subunit TamB"
FT /id="PRO_0000169830"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 7..27
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000250"
FT TOPO_DOM 28..1259
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:25341963"
FT MOD_RES 1
FT /note="N-formylmethionine"
FT /evidence="ECO:0000269|PubMed:22466966"
FT STRAND 977..993
FT /evidence="ECO:0007829|PDB:5VTG"
FT STRAND 1026..1042
FT /evidence="ECO:0007829|PDB:5VTG"
FT STRAND 1045..1058
FT /evidence="ECO:0007829|PDB:5VTG"
FT STRAND 1061..1077
FT /evidence="ECO:0007829|PDB:5VTG"
FT STRAND 1080..1093
FT /evidence="ECO:0007829|PDB:5VTG"
FT STRAND 1099..1105
FT /evidence="ECO:0007829|PDB:5VTG"
FT STRAND 1111..1113
FT /evidence="ECO:0007829|PDB:5VTG"
FT STRAND 1118..1124
FT /evidence="ECO:0007829|PDB:5VTG"
FT STRAND 1129..1135
FT /evidence="ECO:0007829|PDB:5VTG"
SQ SEQUENCE 1259 AA; 136780 MW; CDBB43F0F8C81DB1 CRC64;
MSLWKKISLG VVIVILLLLG SVAFLVGTTS GLHLVFKAAD RWVPGLDIGK VTGGWRDLTL
SDVRYEQPGV AVKAGNLHLA VGLECLWNSS VCINDLALKD IQVNIDSKKM PPSEQVEEEE
DSGPLDLSTP YPITLTRVAL DNVNIKIDDT TVSVMDFTSG LNWQEKTLTL KPTSLKGLLI
ALPKVAEVAQ EEVVEPKIEN PQPDEKPLGE TLKDLFSRPV LPEMTDVHLP LNLNIEEFKG
EQLRVTGDTD ITVSTMLLKV SSIDGNTKLD ALDIDSSQGI VNASGTAQLS DNWPVDITLN
STLNVEPLKG EKVKLKMGGA LREQLEIGVN LSGPVDMDLR AQTRLAEAGL PLNVEVNSKQ
LYWPFTGEKQ YQADDLKLKL TGKMTDYTLS MRTAVKGQEI PPATITLDAK GNEQQVNLDK
LTVAALEGKT ELKALLDWQQ AISWRGELTL NGINTAKEFP DWPSKLNGLI KTRGSLYGGT
WQMDVPELKL TGNVKQNKVN VDGTLKGNSY MQWMIPGLHL ELGPNSAEVK GELGVKDLNL
DATINAPGLD NALPGLGGTA KGLVKVRGTV EAPQLLADIT ARGLRWQELS VAQVRVEGDI
KSTDQIAGKL DVRVEQISQP DVNINLVTLN AKGSEKQHEL QLRIQGEPVS GQLNLAGSFD
RKEERWKGTL SNTRFQTPVG PWSLTRDIAL DYRNKEQKIS IGPHCWLNPN AELCVPQTID
AGAEGRAVVN LNRFDLAMLK PFMPETTQAS GIFTGKADVA WDTTKEGLPQ GSITLSGRNV
QVTQTVNDAA LPVAFQTLNL TAELRNNRAE LGWTIRLTNN GQFDGQVQVT DPQGRRNLGG
NVNIRNFNLA MINPIFTRGE KAAGMVSANL RLGGDVQSPQ LFGQLQVTGV DIDGNFMPFD
MQPSQLAVNF NGMRSTLAGT VRTQQGEIYL NGDADWSQIE NWRARVTAKG SKVRITVPPM
VRMDVSPDVV FEATPNLFTL DGRVDVPWAR IVVHDLPESA VGVSSDVVML NDNLQPEEPK
TASIPINSNL IVHVGNNVRI DAFGLKARLT GDLNVVQDKQ GLGLNGQINI PEGRFHAYGQ
DLIVRKGELL FSGPPDQPYL NIEAIRNPDA TEDDVIAGVR VTGLADEPKA EIFSDPAMSQ
QAALSYLLRG QGLESDQSDS AAMTSMLIGL GVAQSGQIVG KIGETFGVSN LALDTQGVGD
SSQVVVSGYV LPGLQVKYGV GIFDSIATLT LRYRLMPKLY LEAVSGVDQA LDLLYQFEF
