位置:首页 > 蛋白库 > A2MG_ECOLI
A2MG_ECOLI
ID   A2MG_ECOLI              Reviewed;        1653 AA.
AC   P76578; Q2MAH7;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=Alpha-2-macroglobulin {ECO:0000303|PubMed:15186489, ECO:0000303|PubMed:18697741};
DE   AltName: Full=ECAM {ECO:0000303|PubMed:18697741};
DE   Flags: Precursor;
GN   Name=yfhM; OrderedLocusNames=b2520, JW2504;
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=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   [2]
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   [3]
RP   GENE FAMILY.
RX   PubMed=15186489; DOI=10.1186/gb-2004-5-6-r38;
RA   Budd A., Blandin S., Levashina E.A., Gibson T.J.;
RT   "Bacterial alpha2-macroglobulins: colonization factors acquired by
RT   horizontal gene transfer from the metazoan genome?";
RL   Genome Biol. 5:R38.1-R38.13(2004).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND THIOESTER BOND.
RX   PubMed=18697741; DOI=10.1074/jbc.m803127200;
RA   Doan N., Gettins P.G.;
RT   "alpha-macroglobulins are present in some Gram-negative bacteria:
RT   characterization of the alpha2-macroglobulin from Escherichia coli.";
RL   J. Biol. Chem. 283:28747-28756(2008).
RN   [5]
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=21210718; DOI=10.1021/pr101105c;
RA   Maddalo G., Stenberg-Bruzell F., Gotzke H., Toddo S., Bjorkholm P.,
RA   Eriksson H., Chovanec P., Genevaux P., Lehtio J., Ilag L.L., Daley D.O.;
RT   "Systematic analysis of native membrane protein complexes in Escherichia
RT   coli.";
RL   J. Proteome Res. 10:1848-1859(2011).
RN   [6] {ECO:0007744|PDB:4RTD}
RP   X-RAY CRYSTALLOGRAPHY (3.65 ANGSTROMS) OF 23-1653, AND FUNCTION.
RX   PubMed=26143919; DOI=10.1107/s1399004715008548;
RA   Fyfe C.D., Grinter R., Josts I., Mosbahi K., Roszak A.W., Cogdell R.J.,
RA   Wall D.M., Burchmore R.J., Byron O., Walker D.;
RT   "Structure of protease-cleaved Escherichia coli alpha-2-macroglobulin
RT   reveals a putative mechanism of conformational activation for protease
RT   entrapment.";
RL   Acta Crystallogr. D 71:1478-1486(2015).
RN   [7] {ECO:0007744|PDB:4ZIQ, ECO:0007744|PDB:4ZIU, ECO:0007744|PDB:4ZJG, ECO:0007744|PDB:4ZJH, ECO:0007744|PDB:5A42}
RP   X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 163-368, FUNCTION, AND DOMAIN.
RX   PubMed=26100869; DOI=10.1073/pnas.1506538112;
RA   Garcia-Ferrer I., Arede P., Gomez-Blanco J., Luque D., Duquerroy S.,
RA   Caston J.R., Goulas T., Gomis-Ruth F.X.;
RT   "Structural and functional insights into Escherichia coli alpha2-
RT   macroglobulin endopeptidase snap-trap inhibition.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:8290-8295(2015).
CC   -!- FUNCTION: Protects the bacterial cell from host peptidases
CC       (PubMed:18697741, PubMed:26143919, PubMed:26100869). Acts by a
CC       'trapping' mechanism. Cleavage of the bait-region domain by host
CC       peptidases leads to a global conformational change, which results in
CC       entrapment of the host peptidase and activation of the thioester bond
CC       that covalently binds the attacking host peptidase (PubMed:26143919,
CC       PubMed:26100869). Trapped peptidases are still active except against
CC       very large substrates (PubMed:26100869). May protect the entire
CC       periplam, including the lipoproteins anchored to the periplasmic side
CC       of the outer membrane, against intruding endopeptidases
CC       (PubMed:26100869). {ECO:0000269|PubMed:18697741,
CC       ECO:0000269|PubMed:26100869, ECO:0000269|PubMed:26143919}.
CC   -!- SUBUNIT: May form homooligomers. {ECO:0000269|PubMed:21210718}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:18697741,
CC       ECO:0000269|PubMed:21210718}; Lipid-anchor {ECO:0000255|PROSITE-
CC       ProRule:PRU00303}; Periplasmic side {ECO:0000269|PubMed:18697741}.
CC   -!- DOMAIN: Cleavage causes major structural rearrangement of more than
CC       half the 13-domain structure from a native to a compact induced form.
CC       {ECO:0000269|PubMed:26100869}.
CC   -!- MISCELLANEOUS: Bacterial alpha-2-macroglobulins were probably acquired
CC       one or more times by horizontal gene transfer from metazoan hosts.
CC       {ECO:0000305|PubMed:15186489}.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2-
CC       macroglobulin) family. Bacterial alpha-2-macroglobulin subfamily.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U00096; AAC75573.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76729.1; -; Genomic_DNA.
DR   PIR; G65028; G65028.
DR   RefSeq; NP_417015.1; NC_000913.3.
DR   RefSeq; WP_000736312.1; NZ_LN832404.1.
DR   PDB; 4RTD; X-ray; 3.65 A; A=23-1653.
DR   PDB; 4ZIQ; X-ray; 2.55 A; A=40-1653.
DR   PDB; 4ZIU; X-ray; 2.70 A; A=1018-1653.
DR   PDB; 4ZJG; X-ray; 2.30 A; A=40-385.
DR   PDB; 4ZJH; X-ray; 1.60 A; A=163-368.
DR   PDB; 5A42; EM; 16.00 A; A=40-1653.
DR   PDBsum; 4RTD; -.
DR   PDBsum; 4ZIQ; -.
DR   PDBsum; 4ZIU; -.
DR   PDBsum; 4ZJG; -.
DR   PDBsum; 4ZJH; -.
DR   PDBsum; 5A42; -.
DR   AlphaFoldDB; P76578; -.
DR   SMR; P76578; -.
DR   BioGRID; 4260803; 213.
DR   DIP; DIP-28064N; -.
DR   IntAct; P76578; 15.
DR   STRING; 511145.b2520; -.
DR   MEROPS; I39.008; -.
DR   jPOST; P76578; -.
DR   PaxDb; P76578; -.
DR   PRIDE; P76578; -.
DR   EnsemblBacteria; AAC75573; AAC75573; b2520.
DR   EnsemblBacteria; BAE76729; BAE76729; BAE76729.
DR   GeneID; 947302; -.
DR   KEGG; ecj:JW2504; -.
DR   KEGG; eco:b2520; -.
DR   PATRIC; fig|511145.12.peg.2619; -.
DR   EchoBASE; EB3175; -.
DR   eggNOG; COG2373; Bacteria.
DR   HOGENOM; CLU_000965_1_0_6; -.
DR   InParanoid; P76578; -.
DR   OMA; LDRYPYG; -.
DR   PhylomeDB; P76578; -.
DR   BioCyc; EcoCyc:G7323-MON; -.
DR   PRO; PR:P76578; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0031362; C:anchored component of external side of plasma membrane; IDA:EcoCyc.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0004866; F:endopeptidase inhibitor activity; IDA:EcoCyc.
DR   GO; GO:0010951; P:negative regulation of endopeptidase activity; IDA:EcoCyc.
DR   InterPro; IPR026284; A2-macglob_dom_prot_bac.
DR   InterPro; IPR011625; A2M_N_BRD.
DR   InterPro; IPR040639; A2MG_MG1.
DR   InterPro; IPR011626; Alpha-macroglobulin_TED.
DR   InterPro; IPR021868; Alpha_2_Macroglob_MG3.
DR   InterPro; IPR041203; Bact_A2M_MG5.
DR   InterPro; IPR041462; Bact_A2M_MG6.
DR   InterPro; IPR041246; Bact_MG10.
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; PF17970; bMG1; 1.
DR   Pfam; PF17973; bMG10; 1.
DR   Pfam; PF11974; bMG3; 1.
DR   Pfam; PF17972; bMG5; 1.
DR   Pfam; PF17962; bMG6; 1.
DR   Pfam; PF01835; MG2; 1.
DR   Pfam; PF07678; TED_complement; 1.
DR   PIRSF; PIRSF038980; A2M_bac; 1.
DR   SMART; SM01360; A2M; 1.
DR   SMART; SM01359; A2M_N_2; 1.
DR   SUPFAM; SSF48239; SSF48239; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell inner membrane; Cell membrane; Coiled coil; Lipoprotein;
KW   Membrane; Palmitate; Protease inhibitor; Reference proteome; Signal;
KW   Thioester bond.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           18..1653
FT                   /note="Alpha-2-macroglobulin"
FT                   /id="PRO_0000013775"
FT   COILED          1559..1589
FT                   /evidence="ECO:0000255"
FT   LIPID           18
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           18
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CROSSLNK        1187..1190
FT                   /note="Isoglutamyl cysteine thioester (Cys-Gln)"
FT                   /evidence="ECO:0000269|PubMed:18697741"
FT   TURN            58..64
FT                   /evidence="ECO:0007829|PDB:4ZJG"
FT   STRAND          69..77
FT                   /evidence="ECO:0007829|PDB:4ZJG"
FT   STRAND          80..89
FT                   /evidence="ECO:0007829|PDB:4ZJG"
FT   HELIX           97..100
FT                   /evidence="ECO:0007829|PDB:4ZJG"
FT   STRAND          101..105
FT                   /evidence="ECO:0007829|PDB:4ZJG"
FT   TURN            106..108
FT                   /evidence="ECO:0007829|PDB:4ZJG"
FT   STRAND          121..126
FT                   /evidence="ECO:0007829|PDB:4ZJG"
FT   STRAND          134..139
FT                   /evidence="ECO:0007829|PDB:4ZJG"
FT   STRAND          155..160
FT                   /evidence="ECO:0007829|PDB:4ZJG"
FT   STRAND          167..173
FT                   /evidence="ECO:0007829|PDB:4ZJH"
FT   STRAND          175..177
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   HELIX           181..183
FT                   /evidence="ECO:0007829|PDB:4ZJH"
FT   STRAND          185..191
FT                   /evidence="ECO:0007829|PDB:4ZJH"
FT   STRAND          194..202
FT                   /evidence="ECO:0007829|PDB:4ZJH"
FT   HELIX           204..206
FT                   /evidence="ECO:0007829|PDB:4ZJH"
FT   HELIX           207..215
FT                   /evidence="ECO:0007829|PDB:4ZJH"
FT   TURN            216..219
FT                   /evidence="ECO:0007829|PDB:4ZJH"
FT   TURN            222..224
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   HELIX           226..229
FT                   /evidence="ECO:0007829|PDB:4ZJH"
FT   STRAND          232..241
FT                   /evidence="ECO:0007829|PDB:4ZJH"
FT   STRAND          250..254
FT                   /evidence="ECO:0007829|PDB:4ZJH"
FT   HELIX           260..263
FT                   /evidence="ECO:0007829|PDB:4ZJH"
FT   STRAND          266..273
FT                   /evidence="ECO:0007829|PDB:4ZJH"
FT   STRAND          276..278
FT                   /evidence="ECO:0007829|PDB:4ZJG"
FT   STRAND          279..281
FT                   /evidence="ECO:0007829|PDB:4ZJH"
FT   STRAND          284..289
FT                   /evidence="ECO:0007829|PDB:4ZJH"
FT   STRAND          291..299
FT                   /evidence="ECO:0007829|PDB:4ZJH"
FT   STRAND          302..309
FT                   /evidence="ECO:0007829|PDB:4ZJH"
FT   TURN            310..312
FT                   /evidence="ECO:0007829|PDB:4ZJH"
FT   STRAND          320..324
FT                   /evidence="ECO:0007829|PDB:4ZJH"
FT   STRAND          326..328
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          330..335
FT                   /evidence="ECO:0007829|PDB:4ZJH"
FT   STRAND          340..345
FT                   /evidence="ECO:0007829|PDB:4ZJH"
FT   STRAND          352..357
FT                   /evidence="ECO:0007829|PDB:4ZJH"
FT   STRAND          360..365
FT                   /evidence="ECO:0007829|PDB:4ZJH"
FT   STRAND          385..391
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          395..397
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          402..410
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          422..427
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          433..439
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          445..451
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          459..466
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          468..470
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          473..479
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          486..492
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          504..512
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   TURN            513..515
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          522..531
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          553..562
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          567..573
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          584..593
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          599..608
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          610..621
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          623..628
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   TURN            629..632
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          633..641
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          644..653
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          662..671
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          695..704
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          710..715
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          718..726
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          732..740
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   TURN            748..751
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          759..765
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          772..778
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          786..790
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          795..797
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          808..813
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          824..831
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          842..849
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   HELIX           855..857
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          860..864
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          867..869
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          873..882
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   TURN            884..886
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          893..900
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   HELIX           901..904
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   TURN            905..908
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   HELIX           914..919
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          927..931
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   HELIX           932..934
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   HELIX           952..957
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          969..971
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          981..988
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          994..1006
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          1008..1017
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          1020..1026
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          1029..1031
FT                   /evidence="ECO:0007829|PDB:4ZIU"
FT   STRAND          1036..1045
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          1047..1049
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          1051..1061
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          1063..1067
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          1072..1075
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          1080..1089
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          1091..1103
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          1108..1110
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          1115..1124
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          1130..1138
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          1143..1145
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   TURN            1150..1153
FT                   /evidence="ECO:0007829|PDB:4ZIU"
FT   TURN            1156..1158
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          1160..1168
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   HELIX           1173..1175
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          1178..1180
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   HELIX           1188..1193
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   HELIX           1196..1199
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   HELIX           1203..1209
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   HELIX           1216..1232
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          1240..1243
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   HELIX           1251..1266
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   HELIX           1273..1288
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   HELIX           1290..1292
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   HELIX           1301..1317
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   TURN            1318..1320
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   HELIX           1324..1332
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   HELIX           1333..1336
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   HELIX           1340..1353
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   HELIX           1356..1366
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          1379..1381
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   HELIX           1385..1398
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   HELIX           1403..1418
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   HELIX           1425..1435
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   TURN            1436..1440
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          1445..1449
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          1456..1460
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          1462..1467
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   HELIX           1468..1472
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          1475..1478
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          1480..1482
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          1484..1492
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          1494..1496
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          1502..1513
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          1516..1518
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          1523..1525
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          1529..1540
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          1542..1550
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          1555..1557
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   HELIX           1563..1565
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   HELIX           1569..1572
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   HELIX           1574..1576
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   HELIX           1577..1585
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          1586..1593
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          1595..1605
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          1610..1618
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          1622..1624
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          1630..1635
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          1639..1642
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
FT   STRAND          1649..1652
FT                   /evidence="ECO:0007829|PDB:4ZIQ"
SQ   SEQUENCE   1653 AA;  181585 MW;  13109EC5CDEB41A0 CRC64;
     MKKLRVAACM LMLALAGCDN NDNAPTAVKK DAPSEVTKAA SSENASSAKL SVPERQKLAQ
     QSAGKVLTLL DLSEVQLDGA ATLVLTFSIP LDPDQDFSRV IHVVDKKSGK VDGAWELSDN
     LKELRLRHLE PKRDLIVTIG KEVKALNNAT FSKDYEKTIT TRDIQPSVGF ASRGSLLPGK
     VVEGLPVMAL NVNNVDVNFF RVKPESLPAF ISQWEYRNSL ANWQSDKLLQ MADLVYTGRF
     DLNPARNTRE KLLLPLGDIK PLQQAGVYLA VMNQAGRYDY SNPATLFTLS DIGVSAHRYH
     NRLDIFTQSL ENGAAQQGIE VSLLNEKGQT LTQATSDAQG HVQLENDKNA ALLLARKDGQ
     TTLLDLKLPA LDLAEFNIAG APGYSKQFFM FGPRDLYRPG ETVILNGLLR DADGKALPNQ
     PIKLDVIKPD GQVLRSVVSQ PENGLYHFTW PLDSNAATGM WHIRANTGDN QYRMWDFHVE
     DFMPERMALN LTGEKTPLTP KDEVKFSVVG YYLYGAPANG NTLQGQLFLR PLREAVSALP
     GFEFGDIAAE NLSRTLDEVQ LTLDDKGRGE VSTESQWKET HSPLQVIFQG SLLESGGRPV
     TRRAEQAIWP ADALPGIRPQ FASKSVYDYR TDSTVKQPIV DEGSNAAFDI VYSDAQGVKK
     AVSGLQVRLI RERRDYYWNW SEDEGWQSQF DQKDLIENEQ TLDLKADETG KVSFPVEWGA
     YRLEVKAPNE AVSSVRFWAG YSWQDNSDGS GAVRPDRVTL KLDKASYRPG DTIKLHIAAP
     TAGKGYAMVE SSEGPLWWQE IDVRAQGLDL TIPVDKTWNR HDLYLSTLVV RPGDKSRSAT
     PKRAVGVLHL PLGDENRRLD LALETPAKMR PNQPLTVKIK ASTKNGEKPK QVNVLVSAVD
     SGVLNITDYV TPDPWQAFFG QKRYGADIYD IYGQVIEGQG RLAALRFGGD GDELKRGGKP
     PVNHVNIVVQ QALPVTLNEQ GEGSVTLPIG DFNGELRVMA QAWTADDFGS NESKVIVAAP
     VIAELNMPRF MASGDTSRLT LDITNLTDKP QKLNVALTAS GLLELVSDSP AAVELAPGVR
     TTLFIPVRAL PGYGDGEIQA TISGLALPGE TVADQHKQWK IGVRPAFPAQ TVNYGTALQP
     GETWAIPADG LQNFSPVTLE GQLLLSGKPP LNIARYIKEL KAYPYGCLEQ TASGLFPSLY
     TNAAQLQALG IKGDSDEKRR ASVDIGISRL LQMQRDNGGF ALWDKNGDEE YWLTAYVMDF
     LVRAGEQGYS VPTDAINRGN ERLLRYLQDP GMMSIPYADN LKASKFAVQS YAALVLARQQ
     KAPLGALREI WEHRADAASG LPLLQLGVAL KTMGDATRGE EAIALALKTP RNSDERIWLG
     DYGSSLRDNA LMLSLLEENK LLPDEQYTLL NTLSQQAFGE RWLSTQESNA LFLAARTIQD
     LPGKWQAQTS FSAEQLTGEK AQNSNLNSDQ LVTLQVSNSG DQPLWLRMDA SGYPQSAPLP
     ANNVLQIERH ILGTDGKSKS LDSLRSGDLV LVWLQVKASN SVPDALVVDL LPAGLELENQ
     NLANGSASLE QSGGEVQNLL NQMQQASIKH IEFRDDRFVA AVAVDEYQPV TLVYLARAVT
     PGTYQVPQPM VESMYVPQWR ATGAAEDLLI VRP
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024