TMCA_ECOLI
ID TMCA_ECOLI Reviewed; 671 AA.
AC P76562; P76972;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=tRNA(Met) cytidine acetyltransferase TmcA {ECO:0000255|HAMAP-Rule:MF_01886};
DE EC=2.3.1.193 {ECO:0000255|HAMAP-Rule:MF_01886};
DE AltName: Full=Lysine 2-hydroxyisobutyryltransferase {ECO:0000303|PubMed:34903851};
DE EC=2.3.1.- {ECO:0000269|PubMed:34903851};
GN Name=tmcA {ECO:0000255|HAMAP-Rule:MF_01886}; Synonyms=ypfI;
GN OrderedLocusNames=b2474, JW2459;
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 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO
RP 646-671.
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 FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=18668122; DOI=10.1038/emboj.2008.154;
RA Ikeuchi Y., Kitahara K., Suzuki T.;
RT "The RNA acetyltransferase driven by ATP hydrolysis synthesizes N4-
RT acetylcytidine of tRNA anticodon.";
RL EMBO J. 27:2194-2203(2008).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF ARG-319; VAL-463; ARG-469; GLY-471; ARG-502 AND TRP-504.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=34903851; DOI=10.1038/s41589-021-00906-3;
RA Dong H., Zhao Y., Bi C., Han Y., Zhang J., Bai X., Zhai G., Zhang H.,
RA Tian S., Hu D., Xu L., Zhang K.;
RT "TmcA functions as a lysine 2-hydroxyisobutyryltransferase to regulate
RT transcription.";
RL Nat. Chem. Biol. 18:142-151(2022).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH ACETYL-COA AND THE
RP ATP ANALOG ADP, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND
RP MUTAGENESIS OF THR-287; TYR-291; GLU-292; ARG-296; LYS-301; ARG-319;
RP GLU-327; HIS-377; ARG-387 AND ARG-460.
RX PubMed=19322199; DOI=10.1038/emboj.2009.69;
RA Chimnaronk S., Suzuki T., Manita T., Ikeuchi Y., Yao M., Suzuki T.,
RA Tanaka I.;
RT "RNA helicase module in an acetyltransferase that modifies a specific tRNA
RT anticodon.";
RL EMBO J. 28:1362-1373(2009).
CC -!- FUNCTION: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at
CC the wobble position of tRNA(Met), by using acetyl-CoA as an acetyl
CC donor and ATP (or GTP). It recognizes the wobble base of tRNA(Met),
CC thus distinguishing between tRNA(Met) and the structurally similar
CC tRNA(Ile2) (PubMed:18668122, PubMed:19322199). Could use an RNA
CC helicase motor driven by ATP hydrolysis to deliver the wobble base of
CC tRNA(Met) to the acetyltransferase domain of TmcA (Probable).
CC {ECO:0000269|PubMed:18668122, ECO:0000269|PubMed:19322199,
CC ECO:0000305|PubMed:19322199}.
CC -!- FUNCTION: Also functions as a lysine 2-hydroxyisobutyryltransferase to
CC regulate transcription. Can specifically catalyze the 2-
CC hydroxyisobutyrylation (Khib) of the DNA-binding protein H-NS.
CC Hydroxyisobutyrylation of H-NS decreases its DNA-binding activity,
CC promotes the expression of acid-resistance genes and enhances bacterial
CC survival under extreme acid stress. {ECO:0000269|PubMed:34903851}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + ATP + cytidine(34) in elongator tRNA(Met) + H2O =
CC ADP + CoA + H(+) + N(4)-acetylcytidine(34) in elongator tRNA(Met) +
CC phosphate; Xref=Rhea:RHEA:43788, Rhea:RHEA-COMP:10693, Rhea:RHEA-
CC COMP:10694, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:74900, ChEBI:CHEBI:82748, ChEBI:CHEBI:456216;
CC EC=2.3.1.193; Evidence={ECO:0000255|HAMAP-Rule:MF_01886,
CC ECO:0000269|PubMed:18668122, ECO:0000269|PubMed:19322199};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxyisobutanoyl-CoA + L-lysyl-[protein] = CoA + H(+) +
CC N(6)-(2-hydroxyisobutanoyl)-L-lysyl-[protein]; Xref=Rhea:RHEA:24180,
CC Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:15921, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:131780,
CC ChEBI:CHEBI:144968; Evidence={ECO:0000269|PubMed:34903851};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24181;
CC Evidence={ECO:0000269|PubMed:34903851};
CC -!- ACTIVITY REGULATION: ATP/GTP hydrolysis is stimulated by the addition
CC of acetyl-CoA and tRNA(Met). Binding of acetyl-CoA to TmcA activates
CC both ATPase and tRNA-binding activities (PubMed:18668122,
CC PubMed:19322199). ATP promotes the 2-hydroxyisobutyryltransferase
CC activity (PubMed:34903851). {ECO:0000269|PubMed:18668122,
CC ECO:0000269|PubMed:19322199, ECO:0000269|PubMed:34903851}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.93 uM for ATP (in the absence of both acetyl-CoA and tRNA(Met))
CC {ECO:0000269|PubMed:18668122};
CC KM=4.16 uM for ATP (in the presence of both acetyl-CoA and tRNA(Met))
CC {ECO:0000269|PubMed:18668122};
CC KM=117 uM for GTP (in the absence of both acetyl-CoA and tRNA(Met))
CC {ECO:0000269|PubMed:18668122};
CC KM=66.6 uM for GTP (in the presence of both acetyl-CoA and tRNA(Met))
CC {ECO:0000269|PubMed:18668122};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01886}.
CC -!- DISRUPTION PHENOTYPE: Mutants lack the ac(4)C modification, but do not
CC show any growth defects (PubMed:18668122). Knockout mutant shows
CC decreased 2-hydroxyisobutyrylation levels (PubMed:34903851).
CC {ECO:0000269|PubMed:18668122, ECO:0000269|PubMed:34903851}.
CC -!- MISCELLANEOUS: 467 endogenous Khib candidate sites significantly
CC regulated by TmcA were identified in E.coli using a quantitative
CC proteomics approach. {ECO:0000269|PubMed:34903851}.
CC -!- SIMILARITY: Belongs to the RNA cytidine acetyltransferase family. TmcA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01886}.
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DR EMBL; U00096; AAC75527.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16352.2; -; Genomic_DNA.
DR PIR; A65023; A65023.
DR RefSeq; NP_416969.1; NC_000913.3.
DR RefSeq; WP_000829360.1; NZ_LN832404.1.
DR PDB; 2ZPA; X-ray; 2.35 A; A/B=1-671.
DR PDBsum; 2ZPA; -.
DR AlphaFoldDB; P76562; -.
DR SMR; P76562; -.
DR BioGRID; 4259195; 20.
DR DIP; DIP-12825N; -.
DR IntAct; P76562; 8.
DR STRING; 511145.b2474; -.
DR PaxDb; P76562; -.
DR PRIDE; P76562; -.
DR EnsemblBacteria; AAC75527; AAC75527; b2474.
DR EnsemblBacteria; BAA16352; BAA16352; BAA16352.
DR GeneID; 946053; -.
DR KEGG; ecj:JW2459; -.
DR KEGG; eco:b2474; -.
DR PATRIC; fig|1411691.4.peg.4265; -.
DR EchoBASE; EB3948; -.
DR eggNOG; COG1444; Bacteria.
DR HOGENOM; CLU_004652_1_1_6; -.
DR InParanoid; P76562; -.
DR OMA; NEPDDLG; -.
DR PhylomeDB; P76562; -.
DR BioCyc; EcoCyc:G7297-MON; -.
DR BioCyc; MetaCyc:G7297-MON; -.
DR BRENDA; 2.3.1.193; 2026.
DR SABIO-RK; P76562; -.
DR EvolutionaryTrace; P76562; -.
DR PRO; PR:P76562; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0106226; F:peptide 2-hydroxyisobutyryltransferase activity; IEA:RHEA.
DR GO; GO:0000049; F:tRNA binding; IDA:EcoCyc.
DR GO; GO:0051392; F:tRNA N-acetyltransferase activity; IDA:EcoCyc.
DR GO; GO:0051391; P:tRNA acetylation; IMP:EcoCyc.
DR GO; GO:0002101; P:tRNA wobble cytosine modification; IMP:EcoCyc.
DR Gene3D; 1.20.120.890; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01886; tRNA_acetyltr_TmcA; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR007807; Helicase_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032672; TmcA/NAT10/Kre33.
DR InterPro; IPR038321; TmcA_C_sf.
DR InterPro; IPR013562; TmcA_N.
DR InterPro; IPR033442; TmcA_tRNA_bind.
DR InterPro; IPR024914; tRNA_acetyltr_TmcA.
DR PANTHER; PTHR10925; PTHR10925; 2.
DR Pfam; PF08351; DUF1726; 1.
DR Pfam; PF13718; GNAT_acetyltr_2; 1.
DR Pfam; PF05127; Helicase_RecD; 1.
DR Pfam; PF17176; tRNA_bind_3; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; ATP-binding; Cytoplasm; Nucleotide-binding;
KW Reference proteome; RNA-binding; Transferase; tRNA processing;
KW tRNA-binding.
FT CHAIN 1..671
FT /note="tRNA(Met) cytidine acetyltransferase TmcA"
FT /id="PRO_0000169239"
FT DOMAIN 356..531
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT BINDING 180
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886,
FT ECO:0000269|PubMed:19322199"
FT BINDING 202..211
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886,
FT ECO:0000269|PubMed:19322199"
FT BINDING 319
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886,
FT ECO:0000269|PubMed:19322199"
FT BINDING 461..463
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886,
FT ECO:0000269|PubMed:19322199"
FT BINDING 468..474
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886,
FT ECO:0000269|PubMed:19322199"
FT BINDING 499
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886,
FT ECO:0000269|PubMed:19322199"
FT BINDING 506
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886,
FT ECO:0000269|PubMed:19322199"
FT SITE 502
FT /note="Important for lysine 2-hydroxyisobutyryltransferase
FT activity"
FT /evidence="ECO:0000305|PubMed:34903851"
FT MUTAGEN 287
FT /note="T->A: Loss of ATPase activity, but no change in
FT tRNA-binding."
FT /evidence="ECO:0000269|PubMed:19322199"
FT MUTAGEN 291
FT /note="Y->A: Loss of ATPase activity, but no change in
FT tRNA-binding."
FT /evidence="ECO:0000269|PubMed:19322199"
FT MUTAGEN 292
FT /note="E->A: Loss of ATPase activity, but no change in
FT tRNA-binding."
FT /evidence="ECO:0000269|PubMed:19322199"
FT MUTAGEN 296
FT /note="R->A: Decrease in ATPase activity and loss of tRNA-
FT binding."
FT /evidence="ECO:0000269|PubMed:19322199"
FT MUTAGEN 301
FT /note="K->A: Decrease in ATPase activity and loss of tRNA-
FT binding."
FT /evidence="ECO:0000269|PubMed:19322199"
FT MUTAGEN 319
FT /note="R->A: Loss of ATPase activity, but no change in
FT tRNA-binding. Lack of hydroxyisobutyrylation activity."
FT /evidence="ECO:0000269|PubMed:19322199,
FT ECO:0000269|PubMed:34903851"
FT MUTAGEN 327
FT /note="E->A: Loss of ATPase activity, but no change in
FT tRNA-binding."
FT /evidence="ECO:0000269|PubMed:19322199"
FT MUTAGEN 377
FT /note="H->A: Decrease in ATPase activity and loss of tRNA-
FT binding."
FT /evidence="ECO:0000269|PubMed:19322199"
FT MUTAGEN 387
FT /note="R->A: Abolishes the tRNA-binding capacity, but no
FT loss of activity."
FT /evidence="ECO:0000269|PubMed:19322199"
FT MUTAGEN 460
FT /note="R->A: Loss of tRNA-binding."
FT /evidence="ECO:0000269|PubMed:19322199"
FT MUTAGEN 463
FT /note="V->A: Does not affect hydroxyisobutyrylation
FT activity."
FT /evidence="ECO:0000269|PubMed:34903851"
FT MUTAGEN 469
FT /note="R->A: Does not affect hydroxyisobutyrylation
FT activity."
FT /evidence="ECO:0000269|PubMed:34903851"
FT MUTAGEN 471
FT /note="G->A: Does not affect hydroxyisobutyrylation
FT activity."
FT /evidence="ECO:0000269|PubMed:34903851"
FT MUTAGEN 502
FT /note="R->A: Lack of hydroxyisobutyrylation activity. Has
FT little effect on RNA acetylation activity. Alters binding
FT with hydroxyisobutanoyl-CoA, but not with acetyl-CoA."
FT /evidence="ECO:0000269|PubMed:34903851"
FT MUTAGEN 504
FT /note="W->A: Does not affect hydroxyisobutyrylation
FT activity. No change in acetyl-CoA or hydroxyisobutanoyl-CoA
FT binding."
FT /evidence="ECO:0000269|PubMed:34903851"
FT HELIX 3..17
FT /evidence="ECO:0007829|PDB:2ZPA"
FT STRAND 21..27
FT /evidence="ECO:0007829|PDB:2ZPA"
FT HELIX 29..42
FT /evidence="ECO:0007829|PDB:2ZPA"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:2ZPA"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:2ZPA"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:2ZPA"
FT HELIX 86..93
FT /evidence="ECO:0007829|PDB:2ZPA"
FT STRAND 101..107
FT /evidence="ECO:0007829|PDB:2ZPA"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:2ZPA"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:2ZPA"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:2ZPA"
FT HELIX 121..124
FT /evidence="ECO:0007829|PDB:2ZPA"
FT HELIX 133..143
FT /evidence="ECO:0007829|PDB:2ZPA"
FT STRAND 145..153
FT /evidence="ECO:0007829|PDB:2ZPA"
FT HELIX 178..187
FT /evidence="ECO:0007829|PDB:2ZPA"
FT STRAND 192..199
FT /evidence="ECO:0007829|PDB:2ZPA"
FT HELIX 205..215
FT /evidence="ECO:0007829|PDB:2ZPA"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:2ZPA"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:2ZPA"
FT HELIX 231..237
FT /evidence="ECO:0007829|PDB:2ZPA"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:2ZPA"
FT HELIX 246..251
FT /evidence="ECO:0007829|PDB:2ZPA"
FT STRAND 257..262
FT /evidence="ECO:0007829|PDB:2ZPA"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:2ZPA"
FT HELIX 269..276
FT /evidence="ECO:0007829|PDB:2ZPA"
FT STRAND 279..290
FT /evidence="ECO:0007829|PDB:2ZPA"
FT HELIX 296..304
FT /evidence="ECO:0007829|PDB:2ZPA"
FT STRAND 310..313
FT /evidence="ECO:0007829|PDB:2ZPA"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:2ZPA"
FT HELIX 325..333
FT /evidence="ECO:0007829|PDB:2ZPA"
FT HELIX 339..342
FT /evidence="ECO:0007829|PDB:2ZPA"
FT STRAND 350..355
FT /evidence="ECO:0007829|PDB:2ZPA"
FT HELIX 358..361
FT /evidence="ECO:0007829|PDB:2ZPA"
FT HELIX 364..376
FT /evidence="ECO:0007829|PDB:2ZPA"
FT STRAND 377..380
FT /evidence="ECO:0007829|PDB:2ZPA"
FT HELIX 382..390
FT /evidence="ECO:0007829|PDB:2ZPA"
FT STRAND 394..400
FT /evidence="ECO:0007829|PDB:2ZPA"
FT STRAND 402..415
FT /evidence="ECO:0007829|PDB:2ZPA"
FT HELIX 419..426
FT /evidence="ECO:0007829|PDB:2ZPA"
FT HELIX 436..444
FT /evidence="ECO:0007829|PDB:2ZPA"
FT HELIX 450..452
FT /evidence="ECO:0007829|PDB:2ZPA"
FT STRAND 453..463
FT /evidence="ECO:0007829|PDB:2ZPA"
FT STRAND 469..471
FT /evidence="ECO:0007829|PDB:2ZPA"
FT HELIX 472..482
FT /evidence="ECO:0007829|PDB:2ZPA"
FT STRAND 488..495
FT /evidence="ECO:0007829|PDB:2ZPA"
FT HELIX 498..506
FT /evidence="ECO:0007829|PDB:2ZPA"
FT STRAND 510..514
FT /evidence="ECO:0007829|PDB:2ZPA"
FT TURN 520..522
FT /evidence="ECO:0007829|PDB:2ZPA"
FT STRAND 526..532
FT /evidence="ECO:0007829|PDB:2ZPA"
FT HELIX 535..559
FT /evidence="ECO:0007829|PDB:2ZPA"
FT HELIX 575..586
FT /evidence="ECO:0007829|PDB:2ZPA"
FT TURN 591..594
FT /evidence="ECO:0007829|PDB:2ZPA"
FT HELIX 595..604
FT /evidence="ECO:0007829|PDB:2ZPA"
FT HELIX 610..617
FT /evidence="ECO:0007829|PDB:2ZPA"
FT HELIX 622..628
FT /evidence="ECO:0007829|PDB:2ZPA"
FT HELIX 634..650
FT /evidence="ECO:0007829|PDB:2ZPA"
FT HELIX 654..666
FT /evidence="ECO:0007829|PDB:2ZPA"
SQ SEQUENCE 671 AA; 74893 MW; 07C5A019570CDA5D CRC64;
MAELTALHTL TAQMKREGIR RLLVLSGEEG WCFEHTLKLR DALPGDWLWI SPRPDAENHC
SPSALQTLLG REFRHAVFDA RHGFDAAAFA ALSGTLKAGS WLVLLLPVWE EWENQPDADS
LRWSDCPDPI ATPHFVQHLK RVLTADNEAI LWRQNQPFSL AHFTPRTDWY PATGAPQPEQ
QQLLKQLMTM PPGVAAVTAA RGRGKSALAG QLISRIAGRA IVTAPAKAST DVLAQFAGEK
FRFIAPDALL ASDEQADWLV VDEAAAIPAP LLHQLVSRFP RTLLTTTVQG YEGTGRGFLL
KFCARFPHLH RFELQQPIRW AQGCPLEKMV SEALVFDDEN FTHTPQGNIV ISAFEQTLWQ
SDPETPLKVY QLLSGAHYRT SPLDLRRMMD APGQHFLQAA GENEIAGALW LVDEGGLSQQ
LSQAVWAGFR RPRGNLVAQS LAAHGNNPLA ATLRGRRVSR IAVHPARQRE GTGRQLIAGA
LQYTQDLDYL SVSFGYTGEL WRFWQRCGFV LVRMGNHREA SSGCYTAMAL LPMSDAGKQL
AEREHYRLRR DAQALAQWNG ETLPVDPLND AVLSDDDWLE LAGFAFAHRP LLTSLGCLLR
LLQTSELALP ALRGRLQKNA SDAQLCTTLK LSGRKMLLVR QREEAAQALF ALNDVRTERL
RDRITQWQLF H
