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 24-JAN-2024, entry version 156.
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; Pseudomonadota; 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 EMDB; EMD-3016; -.
DR EMDB; EMD-3017; -.
DR EMDB; EMD-3018; -.
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; 511145-b2520; -.
DR EnsemblBacteria; AAC75573; AAC75573; b2520.
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 OrthoDB; 9767116at2; -.
DR PhylomeDB; P76578; -.
DR BioCyc; EcoCyc:G7323-MONOMER; -.
DR PRO; PR:P76578; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IDA:EcoCyc.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:EcoCyc.
DR CDD; cd02891; A2M_like; 1.
DR Gene3D; 1.50.10.20; -; 1.
DR Gene3D; 2.60.40.1930; -; 1.
DR InterPro; IPR026284; A2-macglob_dom_prot_bac.
DR InterPro; IPR049120; A2M_bMG2.
DR InterPro; IPR011625; A2M_N_BRD.
DR InterPro; IPR049122; A2MG_CUB.
DR InterPro; IPR040639; A2MG_MG1.
DR InterPro; IPR047565; Alpha-macroglob_thiol-ester_cl.
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 PANTHER; PTHR40094; ALPHA-2-MACROGLOBULIN HOMOLOG; 1.
DR PANTHER; PTHR40094:SF1; UBIQUITIN DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00207; A2M; 1.
DR Pfam; PF21142; A2M_bMG2; 1.
DR Pfam; PF07703; A2M_BRD; 1.
DR Pfam; PF21765; A2MG_CUB; 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 SMART; SM01419; Thiol-ester_cl; 1.
DR SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 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
//
