A2MGH_ECO57
ID A2MGH_ECO57 Reviewed; 1534 AA.
AC Q8XE35;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Alpha-2-macroglobulin homolog {ECO:0000305};
DE Flags: Precursor;
GN Name=yfaS; OrderedLocusNames=Z3481, ECs3111;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2-
CC macroglobulin) family. Bacterial alpha-2-macroglobulin subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Lacks the conserved thioester bond that is characteristic of
CC the alpha-2-macroglobulins. {ECO:0000305}.
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DR EMBL; AE005174; AAG57357.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB36534.1; -; Genomic_DNA.
DR PIR; A85862; A85862.
DR PIR; G91017; G91017.
DR RefSeq; NP_311138.1; NC_002695.1.
DR AlphaFoldDB; Q8XE35; -.
DR SMR; Q8XE35; -.
DR STRING; 155864.EDL933_3389; -.
DR MEROPS; I39.008; -.
DR EnsemblBacteria; AAG57357; AAG57357; Z3481.
DR EnsemblBacteria; BAB36534; BAB36534; ECs_3111.
DR GeneID; 916819; -.
DR KEGG; ece:Z3481; -.
DR KEGG; ecs:ECs_3111; -.
DR PATRIC; fig|386585.9.peg.3245; -.
DR eggNOG; COG2373; Bacteria.
DR HOGENOM; CLU_004561_0_0_6; -.
DR OMA; YAYYADW; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR011625; A2M_N_BRD.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR001599; Macroglobln_a2.
DR InterPro; IPR002890; MG2.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR Pfam; PF00207; A2M; 1.
DR Pfam; PF07703; A2M_BRD; 1.
DR Pfam; PF01835; MG2; 1.
DR SMART; SM01360; A2M; 1.
DR SMART; SM01359; A2M_N_2; 1.
DR SUPFAM; SSF48239; SSF48239; 1.
PE 3: Inferred from homology;
KW Reference proteome; Signal.
FT SIGNAL 1..38
FT /evidence="ECO:0000255"
FT CHAIN 39..1534
FT /note="Alpha-2-macroglobulin homolog"
FT /id="PRO_0000036240"
SQ SEQUENCE 1534 AA; 169893 MW; E326FD052770F1A3 CRC64;
MDTQRFQSQF HWHLSFKFSG AIAACLSLSL VGTGLANADD SLPSSNYAPP AGGTFFLLAD
SSFSSSEESK VRLEAPGRDY RRYQMEEYGG VDVRLYRIPD PMAFLRQQKN LHRIVVQPQY
LGDGLNNTLT WLWDNWYGKS RRVMQRTFSS QSRQNVTQAL PELQLGNAII KPSRYVQNNQ
FSPLKKYPLV EQFRYPLWQA KPVEPQQGVK LEGASSNFIS PQPGNIYIPL GQQEPGLYLV
EAMVGGYRAT TVVFVSDTVA LSKVSGKELL VWTAGKKQGE AKPGSEILWT DGLGVMTRGV
TDDSGTLQLQ HISPERSYIL GKDAEGGVFV SENFFYESEI YNTRLYIFTD RPLYRAGDRV
DVKVMGREFH DPLHSSPIVS APAKLSVLDA NGSLLQTVDV TLDARNGGQG SFRLPENAVA
GGYELRLAYR NQVYSSSFRV ANYIKPHFEI GLALDKKEFK TGEAVSGKLQ LLYPDGEPVK
NARVQLSLRA QQLSMVGNDL RYAGRFPVSL EGSETVSDAS GHVALNLPAA DKPSRYLLTV
SASDGAAYRV TTTKEILIER GLAHYSLSTA AQYSNSGESV VFRYAALESS KQVPVTYEWL
RLEDRTSHSG DLPSGGKSFT VNFDKPGNYN LTLRDKDGLI LAGLSHAVSG KGSMSHTGTV
DIVADKTLYQ PGETAKMLIT FPEPIDEALL TLERDRVEQQ SLLSHPANWL TLQRLNDTQY
EARVPVSNSF APNITFSVLY TRNGQYSFQN AGIKVAVPQL DIRVKTDKTH YQPGELVNVE
LTSSLKGKPV SAQLTVGVVD EMIYALQPEI APNIGKFFYP LGRNNVRTSS SLSFISYDQA
LSSEPVAPGA TNRSERRVKM LERPRREEVD TAAWMPSLTT DKQGKAYFTF LMPDSLTRWR
ITARGMNGDG LVGQGRAYLR SEKNLYMKWS MPTVYRVGDK PSAGLFIFSQ QDNEPVALVT
KFAGAEMRQT LTLHKGANYI SLAQNIQQSG LLSAELQQNG QVQDSISTKL SFVDNSWPVE
QQKNVMLGGG DNALMLPEQA SNIRLQSSET PQEIFRNNLD ALVDEPWGGV INTGSRLIPL
SLAWRSLADH QSAAANDIRQ MIQDNRLRLM QLAGPGARFT WWGEDGNGDA FLTAWAWYAD
WQASQALGVT QQPEYWQHML DSYAEQADNM PLLHRALVLA WAQEMNLPCK TLLKGLDEAI
ARRGTKTEDF SEEDTRDIND SLILDTPESP LADAVANVLT MTLLKKAQLK STVMPQVQQY
AWDKAVNSNQ PLAHTVVLLN SGGDATQAAA ILSGLTAEQS TIERALAMNW LAKYMATMPS
VVLPAPAGAW AKHKLTGGGE YWRWVGQGVP DILSFGDELS PQNVQVRWRE AAKTAQQSNI
PVTVERQLYR LIPGEEEMSF TLQPVTSNEI DSDALYLDEI TLTSEQDAVL RYGQVEVPLP
PGADVERTTW GISVNKPNAG KQQGQLLEKA RNEMGELAYM VPVKELTGTV TFRHLLRFSQ
KGQFVLPPAR YVRSYAPAQQ SVAAGSEWTG MQVK