AG43_ECOLI
ID AG43_ECOLI Reviewed; 1039 AA.
AC P39180; P75614; P76360; P97241; Q46771;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 3.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Antigen 43;
DE Short=AG43;
DE AltName: Full=Fluffing protein;
DE Contains:
DE RecName: Full=Antigen 43 alpha chain;
DE Contains:
DE RecName: Full=Antigen 43 beta chain;
DE Flags: Precursor;
GN Name=flu; Synonyms=yeeQ, yzzX; OrderedLocusNames=b2000, JW1982;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ML 308-225;
RA Henderson I.R., Owen P.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [3]
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 [4]
RP SEQUENCE REVISION TO 824.
RX PubMed=16397293; DOI=10.1093/nar/gkj405;
RA Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R.,
RA Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T.,
RA Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H.,
RA Thomson N.R., Wishart D., Wanner B.L.;
RT "Escherichia coli K-12: a cooperatively developed annotation snapshot
RT -- 2005.";
RL Nucleic Acids Res. 34:1-9(2006).
RN [5]
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 [6]
RP PRELIMINARY PROTEIN SEQUENCE OF 53-78.
RC STRAIN=ML 308-225;
RX PubMed=2661530; DOI=10.1128/jb.171.7.3634-3640.1989;
RA Caffrey P., Owen P.;
RT "Purification and N-terminal sequence of the alpha subunit of antigen 43, a
RT unique protein complex associated with the outer membrane of Escherichia
RT coli.";
RL J. Bacteriol. 171:3634-3640(1989).
RN [7]
RP PROTEIN SEQUENCE OF 53-63.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [8]
RP GENE NAME.
RX PubMed=9103983; DOI=10.1111/j.1574-6968.1997.tb10317.x;
RA Henderson I.R., Meehan M., Owen P.;
RT "Antigen 43, a phase-variable bipartite outer membrane protein, determines
RT colony morphology and autoaggregation in Escherichia coli K-12.";
RL FEMS Microbiol. Lett. 149:115-120(1997).
RN [9]
RP SUBCELLULAR LOCATION, AND FUNCTION IN AGGREGATION.
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 [10]
RP SUBUNIT, AND DOMAIN.
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).
CC -!- FUNCTION: Controls colony form variation and autoaggregation. May
CC function as an adhesin. {ECO:0000269|PubMed:22466966}.
CC -!- SUBUNIT: Interaction with TamA of the translocation and assembly module
CC (TAM) initiates insertion in the outer membrane (PubMed:25341963).
CC {ECO:0000269|PubMed:25341963}.
CC -!- SUBCELLULAR LOCATION: [Antigen 43]: Periplasm {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Antigen 43 alpha chain]: Secreted. Cell surface
CC {ECO:0000269|PubMed:22466966}. Note=The cell surface component is about
CC 60 kDa and can be released by mild heat treatment (PubMed:22466966).
CC -!- SUBCELLULAR LOCATION: [Antigen 43 beta chain]: Cell outer membrane
CC {ECO:0000305|PubMed:25341963}; Multi-pass membrane protein
CC {ECO:0000305}. Note=May form a beta-barrel.
CC -!- DOMAIN: The signal peptide, cleaved at the inner membrane, guides the
CC autotransporter protein to the periplasmic space. The C-terminal beta
CC chain translocator domain inserts in the outer membrane via TamA
CC (PubMed:25341963). This domain probably forms a hydrophilic pore for
CC the translocation of the passenger domain to the bacterial cell
CC surface, with subsequent cleavage. Finally, the mature protein remains
CC tightly associated with the bacterium (Probable).
CC {ECO:0000269|PubMed:25341963, ECO:0000305}.
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DR EMBL; U24429; AAB47869.1; -; Genomic_DNA.
DR EMBL; U00096; AAT48141.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15825.2; -; Genomic_DNA.
DR RefSeq; WP_000820410.1; NZ_LN832404.1.
DR RefSeq; YP_026164.1; NC_000913.3.
DR AlphaFoldDB; P39180; -.
DR SMR; P39180; -.
DR BioGRID; 4260664; 6.
DR DIP; DIP-2892N; -.
DR IntAct; P39180; 4.
DR STRING; 511145.b2000; -.
DR TCDB; 1.B.12.8.2; the autotransporter-1 (at-1) family.
DR jPOST; P39180; -.
DR PaxDb; P39180; -.
DR PRIDE; P39180; -.
DR EnsemblBacteria; AAT48141; AAT48141; b2000.
DR EnsemblBacteria; BAA15825; BAA15825; BAA15825.
DR GeneID; 946540; -.
DR KEGG; ecj:JW1982; -.
DR KEGG; eco:b2000; -.
DR PATRIC; fig|1411691.4.peg.253; -.
DR EchoBASE; EB2550; -.
DR eggNOG; COG3468; Bacteria.
DR HOGENOM; CLU_009845_1_0_6; -.
DR OMA; FWDSKKK; -.
DR PhylomeDB; P39180; -.
DR BioCyc; EcoCyc:G7080-MON; -.
DR PRO; PR:P39180; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IDA:EcoCyc.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR CDD; cd01344; PL2_Passenger_AT; 1.
DR Gene3D; 2.160.20.20; -; 1.
DR Gene3D; 2.40.128.130; -; 1.
DR InterPro; IPR043990; AC_1.
DR InterPro; IPR030930; AIDA.
DR InterPro; IPR005546; Autotransporte_beta.
DR InterPro; IPR036709; Autotransporte_beta_dom_sf.
DR InterPro; IPR012332; Autotransporter_pectin_lyase_C.
DR InterPro; IPR024973; ESPR.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR Pfam; PF16168; AIDA; 2.
DR Pfam; PF03797; Autotransporter; 1.
DR Pfam; PF13018; ESPR; 1.
DR SMART; SM00869; Autotransporter; 1.
DR SUPFAM; SSF103515; SSF103515; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
DR TIGRFAMs; TIGR04415; O_hepto_targRPT; 5.
DR PROSITE; PS51208; AUTOTRANSPORTER; 1.
PE 1: Evidence at protein level;
KW Cell outer membrane; Direct protein sequencing; Membrane; Periplasm;
KW Reference proteome; Secreted; Signal; Transmembrane;
KW Transmembrane beta strand.
FT SIGNAL 1..52
FT /evidence="ECO:0000269|PubMed:9298646"
FT CHAIN 53..1039
FT /note="Antigen 43"
FT /id="PRO_0000387572"
FT CHAIN 53..551
FT /note="Antigen 43 alpha chain"
FT /id="PRO_0000002696"
FT CHAIN 552..1039
FT /note="Antigen 43 beta chain"
FT /id="PRO_0000002697"
FT DOMAIN 737..1039
FT /note="Autotransporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00556"
FT VARIANT 2
FT /note="K -> N (in strain: ML 308-225)"
FT VARIANT 41..42
FT /note="SL -> FF (in strain: ML 308-225)"
FT VARIANT 46
FT /note="T -> K (in strain: ML 308-225)"
FT VARIANT 157
FT /note="W -> L (in strain: ML 308-225)"
FT VARIANT 188
FT /note="V -> F (in strain: ML 308-225)"
FT VARIANT 303..305
FT /note="ATN -> STI (in strain: ML 308-225)"
FT VARIANT 320
FT /note="A -> T (in strain: ML 308-225)"
FT VARIANT 372
FT /note="N -> Q (in strain: ML 308-225)"
FT VARIANT 493
FT /note="E -> V (in strain: ML 308-225)"
FT VARIANT 497
FT /note="S -> N (in strain: ML 308-225)"
FT VARIANT 585
FT /note="H -> Y (in strain: ML 308-225)"
FT VARIANT 709
FT /note="E -> K (in strain: ML 308-225)"
FT VARIANT 721
FT /note="M -> T (in strain: ML 308-225)"
FT VARIANT 751..753
FT /note="GHL -> SHF (in strain: ML 308-225)"
FT VARIANT 803
FT /note="S -> P (in strain: ML 308-225)"
FT VARIANT 815
FT /note="A -> V (in strain: ML 308-225)"
FT VARIANT 829..835
FT /note="LNLVHTS -> MNLIYNA (in strain: ML 308-225)"
FT VARIANT 845..847
FT /note="QGT -> LGA (in strain: ML 308-225)"
FT VARIANT 855
FT /note="S -> T (in strain: ML 308-225)"
FT VARIANT 888
FT /note="Q -> L (in strain: ML 308-225)"
FT VARIANT 1025
FT /note="S -> I (in strain: ML 308-225)"
FT CONFLICT 61..63
FT /note="ETV -> TTT (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1039 AA; 106825 MW; ABC16C46C264EAED CRC64;
MKRHLNTCYR LVWNHMTGAF VVASELARAR GKRGGVAVAL SLAAVTSLPV LAADIVVHPG
ETVNGGTLAN HDNQIVFGTT NGMTISTGLE YGPDNEANTG GQWVQDGGTA NKTTVTSGGL
QRVNPGGSVS DTVISAGGGQ SLQGRAVNTT LNGGEQWMHE GAIATGTVIN DKGWQVVKPG
TVATDTVVNT GAEGGPDAEN GDTGQFVRGD AVRTTINKNG RQIVRAEGTA NTTVVYAGGD
QTVHGHALDT TLNGGYQYVH NGGTASDTVV NSDGWQIVKN GGVAGNTTVN QKGRLQVDAG
GTATNVTLKQ GGALVTSTAA TVTGINRLGA FSVVEGKADN VVLENGGRLD VLTGHTATNT
RVDDGGTLDV RNGGTATTVS MGNGGVLLAD SGAAVSGTRS DGKAFSIGGG QADALMLEKG
SSFTLNAGDT ATDTTVNGGL FTARGGTLAG TTTLNNGAIL TLSGKTVNND TLTIREGDAL
LQGGSLTGNG SVEKSGSGTL TVSNTTLTQK AVNLNEGTLT LNDSTVTTDV IAQRGTALKL
TGSTVLNGAI DPTNVTLASG ATWNIPDNAT VQSVVDDLSH AGQIHFTSTR TGKFVPATLK
VKNLNGQNGT ISLRVRPDMA QNNADRLVID GGRATGKTIL NLVNAGNSAS GLATSGKGIQ
VVEAINGATT EEGAFVQGNR LQAGAFNYSL NRDSDESWYL RSENAYRAEV PLYASMLTQA
MDYDRIVAGS RSHQTGVNGE NNSVRLSIQG GHLGHDNNGG IARGATPESS GSYGFVRLEG
DLMRTEVAGM SVTAGVYGAA GHSSVDVKDD DGSRAGTVRD DAGSLGGYLN LVHTSSGLWA
DIVAQGTRHS MKASSDNNDF RARGWGWLGS LETGLPFSIT DNLMLEPQLQ YTWQGLSLDD
GKDNAGYVKF GHGSAQHVRA GFRLGSHNDM TFGEGTSSRA PLRDSAKHSV SELPVNWWVQ
PSVIRTFSSR GDMRVGTSTA GSGMTFSPSQ NGTSLDLQAG LEARVRENIT LGVQAGYAHS
VSGSSAEGYN GQATLNVTF
