FTSQ_ECOLI
ID FTSQ_ECOLI Reviewed; 276 AA.
AC P06136;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Cell division protein FtsQ {ECO:0000255|HAMAP-Rule:MF_00911};
GN Name=ftsQ {ECO:0000255|HAMAP-Rule:MF_00911};
GN OrderedLocusNames=b0093, JW0091;
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=K12;
RX PubMed=2995680; DOI=10.1016/0022-2836(85)90290-6;
RA Yi Q.-M., Rockenbach S., Ward J.E. Jr., Lutkenhaus J.;
RT "Structure and expression of the cell division genes ftsQ, ftsA and ftsZ.";
RL J. Mol. Biol. 184:399-412(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=6094474; DOI=10.1128/jb.160.2.546-555.1984;
RA Robinson A.C., Kenan D.J., Hatfull G.F., Sullivan N.F., Spiegelberg R.,
RA Donachie W.D.;
RT "DNA sequence and transcriptional organization of essential cell division
RT genes ftsQ and ftsA of Escherichia coli: evidence for overlapping
RT transcriptional units.";
RL J. Bacteriol. 160:546-555(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2228979; DOI=10.1128/jb.172.11.6611-6614.1990;
RA Dewar S.J., Donachie W.D.;
RT "Regulation of expression of the ftsA cell division gene by sequences in
RT upstream genes.";
RL J. Bacteriol. 172:6611-6614(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA Mizobuchi K., Nakata A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT 2.4 min region.";
RL Nucleic Acids Res. 20:3305-3308(1992).
RN [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
RC STRAIN=K12;
RX PubMed=3528126; DOI=10.1128/jb.167.3.809-817.1986;
RA Robinson A.C., Kenan D.J., Sweeney J., Donachie W.D.;
RT "Further evidence for overlapping transcriptional units in an Escherichia
RT coli cell envelope-cell division gene cluster: DNA sequence and
RT transcriptional organization of the ddl ftsQ region.";
RL J. Bacteriol. 167:809-817(1986).
RN [8]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=2007547; DOI=10.1128/jb.173.7.2187-2195.1991;
RA Carson M.J., Barondess J., Beckwith J.;
RT "The FtsQ protein of Escherichia coli: membrane topology, abundance, and
RT cell division phenotypes due to overproduction and insertion mutations.";
RL J. Bacteriol. 173:2187-2195(1991).
RN [9]
RP SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=9829918; DOI=10.1128/jb.180.23.6107-6116.1998;
RA Buddelmeijer N., Aarsman M.E., Kolk A.H., Vicente M., Nanninga N.;
RT "Localization of cell division protein FtsQ by immunofluorescence
RT microscopy in dividing and nondividing cells of Escherichia coli.";
RL J. Bacteriol. 180:6107-6116(1998).
RN [10]
RP SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=9882666; DOI=10.1128/jb.181.2.521-530.1999;
RA Chen J.C., Weiss D.S., Ghigo J.M., Beckwith J.;
RT "Septal localization of FtsQ, an essential cell division protein in
RT Escherichia coli.";
RL J. Bacteriol. 181:521-530(1999).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=11415986; DOI=10.1093/embo-reports/kve108;
RA Urbanus M.L., Scotti P.A., Froderberg L., Saaf A., de Gier J.W.,
RA Brunner J., Samuelson J.C., Dalbey R.E., Oudega B., Luirink J.;
RT "Sec-dependent membrane protein insertion: sequential interaction of
RT nascent FtsQ with SecY and YidC.";
RL EMBO Rep. 2:524-529(2001).
RN [12]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=11703663; DOI=10.1046/j.1365-2958.2001.02640.x;
RA Chen J.C., Beckwith J.;
RT "FtsQ, FtsL and FtsI require FtsK, but not FtsN, for co-localization with
RT FtsZ during Escherichia coli cell division.";
RL Mol. Microbiol. 42:395-413(2001).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=11948172; DOI=10.1128/jb.184.9.2552-2556.2002;
RA Hale C.A., de Boer P.A.J.;
RT "ZipA is required for recruitment of FtsK, FtsQ, FtsL, and FtsN to the
RT septal ring in Escherichia coli.";
RL J. Bacteriol. 184:2552-2556(2002).
RN [14]
RP SUBUNIT, INTERACTION WITH FTSL AND FTSB, AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=15165235; DOI=10.1111/j.1365-2958.2004.04044.x;
RA Buddelmeijer N., Beckwith J.;
RT "A complex of the Escherichia coli cell division proteins FtsL, FtsB and
RT FtsQ forms independently of its localization to the septal region.";
RL Mol. Microbiol. 52:1315-1327(2004).
RN [15]
RP INTERACTION WITH FTSL; FTSA; FTSI; FTSN; FTSX AND YMGF.
RC STRAIN=K12;
RX PubMed=15774864; DOI=10.1128/jb.187.7.2233-2243.2005;
RA Karimova G., Dautin N., Ladant D.;
RT "Interaction network among Escherichia coli membrane proteins involved in
RT cell division as revealed by bacterial two-hybrid analysis.";
RL J. Bacteriol. 187:2233-2243(2005).
RN [16]
RP SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF LEU-29; LEU-32 AND VAL-38.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=17693520; DOI=10.1128/jb.00723-07;
RA Scheffers D.J., Robichon C., Haan G.J., den Blaauwen T., Koningstein G.,
RA van Bloois E., Beckwith J., Luirink J.;
RT "Contribution of the FtsQ transmembrane segment to localization to the cell
RT division site.";
RL J. Bacteriol. 189:7273-7280(2007).
RN [17]
RP FUNCTION, SUBUNIT, DOMAIN, AND INTERACTION WITH FTSK; FTSW; FTSI AND FTSN.
RC STRAIN=K12;
RX PubMed=17185541; DOI=10.1099/mic.0.2006/000265-0;
RA D'Ulisse V., Fagioli M., Ghelardini P., Paolozzi L.;
RT "Three functional subdomains of the Escherichia coli FtsQ protein are
RT involved in its interaction with the other division proteins.";
RL Microbiology 153:124-138(2007).
RN [18]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH FTSB.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=19233928; DOI=10.1128/jb.01597-08;
RA Gonzalez M.D., Beckwith J.;
RT "Divisome under construction: distinct domains of the small membrane
RT protein FtsB are necessary for interaction with multiple cell division
RT proteins.";
RL J. Bacteriol. 191:2815-2825(2009).
RN [19]
RP INDUCTION BY HYDROXYUREA.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=20005847; DOI=10.1016/j.molcel.2009.11.024;
RA Davies B.W., Kohanski M.A., Simmons L.A., Winkler J.A., Collins J.J.,
RA Walker G.C.;
RT "Hydroxyurea induces hydroxyl radical-mediated cell death in Escherichia
RT coli.";
RL Mol. Cell 36:845-860(2009).
RN [20]
RP 3D-STRUCTURE MODELING OF THE FTSB/FTSL/FTSQ COMPLEX.
RX PubMed=21672257; DOI=10.1186/1472-6807-11-28;
RA Villanelo F., Ordenes A., Brunet J., Lagos R., Monasterio O.;
RT "A model for the Escherichia coli FtsB/FtsL/FtsQ cell division complex.";
RL BMC Struct. Biol. 11:28-28(2011).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 58-276, DOMAIN, AND MUTAGENESIS OF
RP ASP-91; LYS-113; GLU-125 AND ASP-237.
RX PubMed=18312270; DOI=10.1111/j.1365-2958.2008.06141.x;
RA van den Ent F., Vinkenvleugel T.M., Ind A., West P., Veprintsev D.,
RA Nanninga N., den Blaauwen T., Lowe J.;
RT "Structural and mutational analysis of the cell division protein FtsQ.";
RL Mol. Microbiol. 68:110-123(2008).
RN [22]
RP STRUCTURE BY NMR OF 22-103.
RX PubMed=21499241; DOI=10.1038/nsmb.2026;
RA Frauenfeld J., Gumbart J., Sluis E.O., Funes S., Gartmann M., Beatrix B.,
RA Mielke T., Berninghausen O., Becker T., Schulten K., Beckmann R.;
RT "Cryo-EM structure of the ribosome-SecYE complex in the membrane
RT environment.";
RL Nat. Struct. Mol. Biol. 18:614-621(2011).
CC -!- FUNCTION: Essential cell division protein. May link together the
CC upstream cell division proteins, which are predominantly cytoplasmic,
CC with the downstream cell division proteins, which are predominantly
CC periplasmic. May control correct divisome assembly. {ECO:0000255|HAMAP-
CC Rule:MF_00911, ECO:0000269|PubMed:17185541,
CC ECO:0000269|PubMed:19233928}.
CC -!- SUBUNIT: Part of a complex composed of FtsB, FtsL and FtsQ. The complex
CC can be formed before its localization to the division site. This
CC tripartite complex can be divided further into a subcomplex of FtsB and
CC FtsL, which forms in the absence of FtsQ. Interacts with FtsA, FtsK,
CC FtsL, FtsB, FtsW, FtsI, FtsN, FtsX and YmgF. {ECO:0000255|HAMAP-
CC Rule:MF_00911, ECO:0000269|PubMed:15165235,
CC ECO:0000269|PubMed:15774864, ECO:0000269|PubMed:17185541,
CC ECO:0000269|PubMed:19233928}.
CC -!- INTERACTION:
CC P06136; P0A6S5: ftsB; NbExp=10; IntAct=EBI-1130157, EBI-1113953;
CC P06136; P0AD68: ftsI; NbExp=5; IntAct=EBI-1130157, EBI-548564;
CC P06136; P46889: ftsK; NbExp=3; IntAct=EBI-1130157, EBI-550795;
CC P06136; P0AEN4: ftsL; NbExp=12; IntAct=EBI-1130157, EBI-1119082;
CC P06136; P29131: ftsN; NbExp=7; IntAct=EBI-1130157, EBI-1134233;
CC P06136; P06136: ftsQ; NbExp=6; IntAct=EBI-1130157, EBI-1130157;
CC P06136; P0ABG4: ftsW; NbExp=4; IntAct=EBI-1130157, EBI-1214767;
CC P06136; P58034: ymgF; NbExp=3; IntAct=EBI-1130157, EBI-1214577;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00911, ECO:0000269|PubMed:11415986,
CC ECO:0000269|PubMed:11703663, ECO:0000269|PubMed:11948172,
CC ECO:0000269|PubMed:15165235, ECO:0000269|PubMed:17693520,
CC ECO:0000269|PubMed:2007547, ECO:0000269|PubMed:9829918,
CC ECO:0000269|PubMed:9882666}; Single-pass type II membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00911, ECO:0000269|PubMed:11415986,
CC ECO:0000269|PubMed:11703663, ECO:0000269|PubMed:11948172,
CC ECO:0000269|PubMed:15165235, ECO:0000269|PubMed:17693520,
CC ECO:0000269|PubMed:2007547, ECO:0000269|PubMed:9829918,
CC ECO:0000269|PubMed:9882666}. Note=Localizes to the division septum.
CC Localization requires FtsZ, FtsA, ZipA and FtsK, but not FtsL, FtsI and
CC FtsN. Insertion into the membrane requires YidC and the Sec
CC translocase.
CC -!- INDUCTION: Repressed by hydroxyurea. {ECO:0000269|PubMed:20005847}.
CC -!- DOMAIN: The C-terminal periplasmic region is necessary and sufficient
CC for septal targeting. The transmembrane region contributes to
CC localization to the cell division site. Three periplasmic subdomains
CC are involved in the interactions with other cell division proteins.
CC Localization and recruitment require two separate domains.
CC {ECO:0000269|PubMed:17185541, ECO:0000269|PubMed:17693520,
CC ECO:0000269|PubMed:18312270, ECO:0000269|PubMed:9829918,
CC ECO:0000269|PubMed:9882666}.
CC -!- SIMILARITY: Belongs to the FtsQ/DivIB family. FtsQ subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00911}.
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; M14029; AAA23673.1; -; Genomic_DNA.
DR EMBL; K02668; AAA23816.1; -; Genomic_DNA.
DR EMBL; X55034; CAA38870.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73204.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96661.1; -; Genomic_DNA.
DR PIR; S10852; CEECQ.
DR RefSeq; NP_414635.1; NC_000913.3.
DR RefSeq; WP_000075748.1; NZ_SSZK01000004.1.
DR PDB; 2VH1; X-ray; 2.70 A; A/B=58-276.
DR PDB; 4UE4; EM; 7.00 A; B=29-50.
DR PDB; 4V6M; EM; 7.10 A; Z=22-103.
DR PDB; 5Z2W; X-ray; 3.00 A; A=53-261.
DR PDB; 6H9N; X-ray; 2.60 A; A=57-276.
DR PDB; 6H9O; X-ray; 2.80 A; A/C=57-276.
DR PDBsum; 2VH1; -.
DR PDBsum; 4UE4; -.
DR PDBsum; 4V6M; -.
DR PDBsum; 5Z2W; -.
DR PDBsum; 6H9N; -.
DR PDBsum; 6H9O; -.
DR AlphaFoldDB; P06136; -.
DR SMR; P06136; -.
DR BioGRID; 4261112; 336.
DR BioGRID; 849224; 4.
DR ComplexPortal; CPX-3099; FtsQBL complex.
DR DIP; DIP-9706N; -.
DR IntAct; P06136; 19.
DR MINT; P06136; -.
DR STRING; 511145.b0093; -.
DR PaxDb; P06136; -.
DR PRIDE; P06136; -.
DR EnsemblBacteria; AAC73204; AAC73204; b0093.
DR EnsemblBacteria; BAB96661; BAB96661; BAB96661.
DR GeneID; 944823; -.
DR KEGG; ecj:JW0091; -.
DR KEGG; eco:b0093; -.
DR PATRIC; fig|1411691.4.peg.2187; -.
DR EchoBASE; EB0338; -.
DR eggNOG; COG1589; Bacteria.
DR HOGENOM; CLU_064041_2_1_6; -.
DR InParanoid; P06136; -.
DR OMA; MARIQRF; -.
DR PhylomeDB; P06136; -.
DR BioCyc; EcoCyc:EG10342-MON; -.
DR EvolutionaryTrace; P06136; -.
DR PRO; PR:P06136; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0032153; C:cell division site; IDA:EcoCyc.
DR GO; GO:1990586; C:divisome complex; IC:ComplexPortal.
DR GO; GO:1990587; C:FtsQBL complex; IPI:ComplexPortal.
DR GO; GO:0016021; C:integral component of membrane; IDA:EcoliWiki.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0051301; P:cell division; IMP:EcoliWiki.
DR GO; GO:0000917; P:division septum assembly; IMP:EcoliWiki.
DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IMP:EcoCyc.
DR Gene3D; 3.40.50.11690; -; 1.
DR HAMAP; MF_00911; FtsQ_subfam; 1.
DR InterPro; IPR005548; Cell_div_FtsQ/DivIB_C.
DR InterPro; IPR026579; FtsQ.
DR InterPro; IPR045335; FtsQ_C_sf.
DR InterPro; IPR034746; POTRA.
DR InterPro; IPR013685; POTRA_FtsQ_type.
DR PANTHER; PTHR35851; PTHR35851; 1.
DR Pfam; PF03799; FtsQ; 1.
DR Pfam; PF08478; POTRA_1; 1.
DR PROSITE; PS51779; POTRA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cell inner membrane;
KW Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..276
FT /note="Cell division protein FtsQ"
FT /id="PRO_0000160580"
FT TOPO_DOM 1..27
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00911"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00911"
FT TOPO_DOM 49..276
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00911"
FT DOMAIN 55..126
FT /note="POTRA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01115"
FT REGION 255..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 29
FT /note="L->R: No change in activity. Correctly assembled,
FT interacts with FtsB and FtsL, but fails to localize
FT efficiently to the cell division site; when associated with
FT R-32. Does not insert into the membrane and lack of
FT activity; when associated with R-32 and P-38."
FT /evidence="ECO:0000269|PubMed:17693520"
FT MUTAGEN 32
FT /note="L->R: No change in activity. Correctly assembled,
FT interacts with FtsB and FtsL, but fails to localize
FT efficiently to the cell division site; when associated with
FT R-29. Does not insert into the membrane and lack of
FT activity; when associated with R-29 and P-38."
FT /evidence="ECO:0000269|PubMed:17693520"
FT MUTAGEN 38
FT /note="V->P: No change in activity. Does not insert into
FT the membrane and lack of activity; when associated with R-
FT 29 and R-32."
FT /evidence="ECO:0000269|PubMed:17693520"
FT MUTAGEN 91
FT /note="D->K,Q: Does not affect localization."
FT /evidence="ECO:0000269|PubMed:18312270"
FT MUTAGEN 113
FT /note="K->D: Impairs localization."
FT /evidence="ECO:0000269|PubMed:18312270"
FT MUTAGEN 125
FT /note="E->K: Impairs localization."
FT /evidence="ECO:0000269|PubMed:18312270"
FT MUTAGEN 237
FT /note="D->N: Localizes to mid-cell, but is unable to form a
FT functional complex with FtsL/FtsB."
FT /evidence="ECO:0000269|PubMed:18312270"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:6H9N"
FT HELIX 71..79
FT /evidence="ECO:0007829|PDB:6H9N"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:5Z2W"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:2VH1"
FT HELIX 92..102
FT /evidence="ECO:0007829|PDB:6H9N"
FT STRAND 106..114
FT /evidence="ECO:0007829|PDB:6H9N"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:6H9N"
FT STRAND 118..125
FT /evidence="ECO:0007829|PDB:6H9N"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:6H9N"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:6H9N"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:6H9N"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:6H9O"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:6H9N"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:6H9N"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:6H9N"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:5Z2W"
FT HELIX 167..182
FT /evidence="ECO:0007829|PDB:6H9N"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:6H9N"
FT STRAND 188..193
FT /evidence="ECO:0007829|PDB:6H9N"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:2VH1"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:6H9N"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:2VH1"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:6H9N"
FT HELIX 216..236
FT /evidence="ECO:0007829|PDB:6H9N"
FT STRAND 239..245
FT /evidence="ECO:0007829|PDB:6H9N"
FT STRAND 248..258
FT /evidence="ECO:0007829|PDB:6H9N"
SQ SEQUENCE 276 AA; 31434 MW; 839A3D34B948CEAB CRC64;
MSQAALNTRN SEEEVSSRRN NGTRLAGILF LLTVLTTVLV SGWVVLGWME DAQRLPLSKL
VLTGERHYTR NDDIRQSILA LGEPGTFMTQ DVNIIQTQIE QRLPWIKQVS VRKQWPDELK
IHLVEYVPIA RWNDQHMVDA EGNTFSVPPE RTSKQVLPML YGPEGSANEV LQGYREMGQM
LAKDRFTLKE AAMTARRSWQ LTLNNDIKLN LGRGDTMKRL ARFVELYPVL QQQAQTDGKR
ISYVDLRYDS GAAVGWAPLP PEESTQQQNQ AQAEQQ
