FTSN_ECOLI
ID FTSN_ECOLI Reviewed; 319 AA.
AC P29131; Q2M8M9;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2003, sequence version 3.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Cell division protein FtsN {ECO:0000255|HAMAP-Rule:MF_02039, ECO:0000305};
GN Name=ftsN {ECO:0000255|HAMAP-Rule:MF_02039}; Synonyms=msgA;
GN OrderedLocusNames=b3933, JW3904;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8509333; DOI=10.1128/jb.175.12.3790-3797.1993;
RA Dai K., Xu Y., Lutkenhaus J.;
RT "Cloning and characterization of ftsN, an essential cell division gene in
RT Escherichia coli isolated as a multicopy suppressor of ftsA12(Ts).";
RL J. Bacteriol. 175:3790-3797(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=XPH43;
RA Wu B., Ang D.;
RL Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8346018; DOI=10.1093/nar/21.15.3391;
RA Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT from 87.2 to 89.2 minutes.";
RL Nucleic Acids Res. 21:3391-3398(1993).
RN [4]
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 [5]
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 [6]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RC STRAIN=K12;
RX PubMed=8631709; DOI=10.1128/jb.178.5.1328-1334.1996;
RA Dai K., Xu Y., Lutkenhaus J.;
RT "Topological characterization of the essential Escherichia coli cell
RT division protein FtsN.";
RL J. Bacteriol. 178:1328-1334(1996).
RN [7]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12;
RX PubMed=9282742; DOI=10.1046/j.1365-2958.1997.4641833.x;
RA Addinall S.G., Cao C., Lutkenhaus J.;
RT "FtsN, a late recruit to the septum in Escherichia coli.";
RL Mol. Microbiol. 25:303-309(1997).
RN [8]
RP DISRUPTION PHENOTYPE.
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 [9]
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 [10]
RP FUNCTION IN RECRUITMENT OF AMIC.
RC STRAIN=K12;
RX PubMed=12787347; DOI=10.1046/j.1365-2958.2003.03511.x;
RA Bernhardt T.G., de Boer P.A.;
RT "The Escherichia coli amidase AmiC is a periplasmic septal ring component
RT exported via the twin-arginine transport pathway.";
RL Mol. Microbiol. 48:1171-1182(2003).
RN [11]
RP DOMAIN, AND BINDING TO PEPTIDOGLYCAN.
RX PubMed=15466024; DOI=10.1128/jb.186.20.6728-6737.2004;
RA Ursinus A., van den Ent F., Brechtel S., de Pedro M., Hoeltje J.V.,
RA Loewe J., Vollmer W.;
RT "Murein (peptidoglycan) binding property of the essential cell division
RT protein FtsN from Escherichia coli.";
RL J. Bacteriol. 186:6728-6737(2004).
RN [12]
RP INTERACTION WITH FTSQ.
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 [13]
RP SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=19684127; DOI=10.1128/jb.00811-09;
RA Gerding M.A., Liu B., Bendezu F.O., Hale C.A., Bernhardt T.G.,
RA de Boer P.A.;
RT "Self-enhanced accumulation of FtsN at division sites and roles for other
RT proteins with a SPOR domain (DamX, DedD, and RlpA) in Escherichia coli cell
RT constriction.";
RL J. Bacteriol. 191:7383-7401(2009).
RN [14]
RP INTERACTION WITH ZAPA; FTSW AND FTSI.
RX PubMed=20497333; DOI=10.1111/j.1365-2958.2010.07211.x;
RA Alexeeva S., Gadella T.W. Jr., Verheul J., Verhoeven G.S., den Blaauwen T.;
RT "Direct interactions of early and late assembling division proteins in
RT Escherichia coli cells resolved by FRET.";
RL Mol. Microbiol. 77:384-398(2010).
RN [15]
RP DISRUPTION PHENOTYPE.
RX PubMed=20345660; DOI=10.1111/j.1365-2958.2010.07134.x;
RA Rico A.I., Garcia-Ovalle M., Palacios P., Casanova M., Vicente M.;
RT "Role of Escherichia coli FtsN protein in the assembly and stability of the
RT cell division ring.";
RL Mol. Microbiol. 76:760-771(2010).
RN [16]
RP INTERACTION WITH FTSA.
RX PubMed=22328664; DOI=10.1128/jb.06683-11;
RA Busiek K.K., Eraso J.M., Wang Y., Margolin W.;
RT "The early divisome protein FtsA interacts directly through its 1c
RT subdomain with the cytoplasmic domain of the late divisome protein FtsN.";
RL J. Bacteriol. 194:1989-2000(2012).
RN [17]
RP DOMAIN, DISULFIDE BOND, AND MUTAGENESIS OF GLN-251; CYS-252; SER-254;
RP THR-263; PHE-270; TRP-283; ARG-285; CYS-312 AND ILE-313.
RX PubMed=24056104; DOI=10.1128/jb.00911-13;
RA Duncan T.R., Yahashiri A., Arends S.J., Popham D.L., Weiss D.S.;
RT "Identification of SPOR domain amino acids important for septal
RT localization, peptidoglycan binding, and a disulfide bond in the cell
RT division protein FtsN.";
RL J. Bacteriol. 195:5308-5315(2013).
RN [18]
RP INTERACTION WITH FTSA, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=24750258; DOI=10.1111/mmi.12623;
RA Busiek K.K., Margolin W.;
RT "A role for FtsA in SPOR-independent localization of the essential
RT Escherichia coli cell division protein FtsN.";
RL Mol. Microbiol. 92:1212-1226(2014).
RN [19]
RP FUNCTION.
RX PubMed=25496050; DOI=10.1111/mmi.12905;
RA Tsang M.J., Bernhardt T.G.;
RT "A role for the FtsQLB complex in cytokinetic ring activation revealed by
RT an ftsL allele that accelerates division.";
RL Mol. Microbiol. 95:925-944(2015).
RN [20]
RP FUNCTION, INTERACTION WITH FTSA, AND MUTAGENESIS OF TRP-83; TYR-85 AND
RP LEU-89.
RX PubMed=25496160; DOI=10.1111/mmi.12906;
RA Liu B., Persons L., Lee L., de Boer P.A.;
RT "Roles for both FtsA and the FtsBLQ subcomplex in FtsN-stimulated cell
RT constriction in Escherichia coli.";
RL Mol. Microbiol. 95:945-970(2015).
RN [21]
RP INTERACTION WITH FTSA, AND MUTAGENESIS OF ASP-5.
RX PubMed=25496259; DOI=10.1111/mmi.12907;
RA Pichoff S., Du S., Lutkenhaus J.;
RT "The bypass of ZipA by overexpression of FtsN requires a previously unknown
RT conserved FtsN motif essential for FtsA-FtsN interaction supporting a model
RT in which FtsA monomers recruit late cell division proteins to the Z ring.";
RL Mol. Microbiol. 95:971-987(2015).
RN [22]
RP FUNCTION, AND REVIEW.
RX PubMed=25571948; DOI=10.1111/mmi.12925;
RA Weiss D.S.;
RT "Last but not least: new insights into how FtsN triggers constriction
RT during Escherichia coli cell division.";
RL Mol. Microbiol. 95:903-909(2015).
RN [23]
RP STRUCTURE BY NMR OF 243-319, AND DOMAIN.
RX PubMed=15101973; DOI=10.1111/j.1365-2958.2004.03991.x;
RA Yang J.C., Van Den Ent F., Neuhaus D., Brevier J., Lowe J.;
RT "Solution structure and domain architecture of the divisome protein FtsN.";
RL Mol. Microbiol. 52:651-660(2004).
CC -!- FUNCTION: Essential cell division protein that activates septal
CC peptidoglycan synthesis and constriction of the cell. Acts on both
CC sides of the membrane, via interaction with FtsA in the cytoplasm and
CC interaction with the FtsQBL complex in the periplasm. These
CC interactions may induce a conformational switch in both FtsA and
CC FtsQBL, leading to septal peptidoglycan synthesis by FtsI and
CC associated synthases (Probable) (PubMed:25496160). Required for full
CC FtsI activity (PubMed:25496160). Required for recruitment of AmiC to
CC the septal ring (PubMed:12787347). {ECO:0000269|PubMed:12787347,
CC ECO:0000269|PubMed:25496160, ECO:0000305|PubMed:25496050,
CC ECO:0000305|PubMed:25571948}.
CC -!- SUBUNIT: Interacts with FtsA via its N-terminal cytoplasmic domain
CC (PubMed:22328664, PubMed:24750258, PubMed:25496160, PubMed:25496259).
CC Interacts with ZapA, FtsQ, FtsW and FtsI (PubMed:17185541,
CC PubMed:20497333). {ECO:0000269|PubMed:17185541,
CC ECO:0000269|PubMed:20497333, ECO:0000269|PubMed:22328664,
CC ECO:0000269|PubMed:24750258, ECO:0000269|PubMed:25496160,
CC ECO:0000269|PubMed:25496259}.
CC -!- INTERACTION:
CC P29131; P56976: blr; NbExp=3; IntAct=EBI-1134233, EBI-6419495;
CC P29131; P0ABH0: ftsA; NbExp=7; IntAct=EBI-1134233, EBI-550562;
CC P29131; P0AD68: ftsI; NbExp=3; IntAct=EBI-1134233, EBI-548564;
CC P29131; P06136: ftsQ; NbExp=7; IntAct=EBI-1134233, EBI-1130157;
CC P29131; P0ABG4: ftsW; NbExp=3; IntAct=EBI-1134233, EBI-1214767;
CC P29131; P02919: mrcB; NbExp=7; IntAct=EBI-1134233, EBI-909769;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:8631709};
CC Single-pass type II membrane protein {ECO:0000269|PubMed:8631709}.
CC Note=Localizes to the septum (PubMed:9282742, PubMed:19684127,
CC PubMed:24750258). Localizes to the midcell via interaction with the
CC early cell division protein FtsA and via the periplasmic SPOR domain
CC (PubMed:9282742, PubMed:19684127, PubMed:24750258). FtsA-dependent
CC localization precedes SPOR-dependent localization, and both are needed
CC for efficient localization (PubMed:24750258). Localization depends upon
CC FtsZ, FtsA, ZipA, FtsQ and FtsI (PubMed:9282742, PubMed:11948172).
CC {ECO:0000269|PubMed:11948172, ECO:0000269|PubMed:19684127,
CC ECO:0000269|PubMed:24750258, ECO:0000269|PubMed:9282742}.
CC -!- DOMAIN: The cytoplasmic region is required for interaction with FtsA
CC (PubMed:24750258). The periplasmic region is composed of a membrane-
CC proximal region containing three short partially formed helices (H1, H2
CC and H3), followed by an unstructured glutamine-rich linker, and a C-
CC terminal globular SPOR domain (PubMed:15101973, PubMed:19684127).
CC Essential function of FtsN is accomplished by a small region of at most
CC 35 residues that is centered about the H2 helix (PubMed:19684127). The
CC SPOR domain, which exhibits a ribonucleoprotein (RNP) fold, binds
CC peptidoglycan and is a strong septal localization determinant, but it
CC seems not essential for cell division (PubMed:15466024,
CC PubMed:19684127, PubMed:24056104). {ECO:0000269|PubMed:15101973,
CC ECO:0000269|PubMed:15466024, ECO:0000269|PubMed:19684127,
CC ECO:0000269|PubMed:24056104, ECO:0000269|PubMed:24750258}.
CC -!- DISRUPTION PHENOTYPE: Depletion does not affect localization of FtsZ,
CC FtsA, ZipA, FtsQ, FtsL and FtsI to the division site (PubMed:11703663).
CC Cells containing low levels of FtsN stop dividing while their mean cell
CC length increases (PubMed:20345660). Absence of FtsN is followed by an
CC inverse sequential disassembly of already assembled divisome compounds
CC (PubMed:20345660). {ECO:0000269|PubMed:11703663,
CC ECO:0000269|PubMed:20345660}.
CC -!- SIMILARITY: Belongs to the FtsN family. {ECO:0000255|HAMAP-
CC Rule:MF_02039, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA23935.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L14281; AAA23814.1; -; Genomic_DNA.
DR EMBL; L06547; AAA23935.1; ALT_FRAME; Genomic_DNA.
DR EMBL; L19201; AAB03065.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76915.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77377.1; -; Genomic_DNA.
DR PIR; S40876; S40876.
DR RefSeq; NP_418368.1; NC_000913.3.
DR RefSeq; WP_000068828.1; NZ_SSZK01000014.1.
DR PDB; 1UTA; NMR; -; A=243-319.
DR PDB; 6YN0; X-ray; 2.40 A; B=75-93.
DR PDBsum; 1UTA; -.
DR PDBsum; 6YN0; -.
DR AlphaFoldDB; P29131; -.
DR BMRB; P29131; -.
DR SMR; P29131; -.
DR BioGRID; 4261592; 198.
DR BioGRID; 852725; 3.
DR ComplexPortal; CPX-1936; Divisome complex.
DR DIP; DIP-9705N; -.
DR IntAct; P29131; 24.
DR MINT; P29131; -.
DR STRING; 511145.b3933; -.
DR jPOST; P29131; -.
DR PaxDb; P29131; -.
DR PRIDE; P29131; -.
DR EnsemblBacteria; AAC76915; AAC76915; b3933.
DR EnsemblBacteria; BAE77377; BAE77377; BAE77377.
DR GeneID; 948428; -.
DR KEGG; ecj:JW3904; -.
DR KEGG; eco:b3933; -.
DR PATRIC; fig|511145.12.peg.4051; -.
DR EchoBASE; EB1491; -.
DR eggNOG; COG3087; Bacteria.
DR HOGENOM; CLU_058902_0_0_6; -.
DR InParanoid; P29131; -.
DR OMA; NRPEEVW; -.
DR PhylomeDB; P29131; -.
DR BioCyc; EcoCyc:EG11529-MON; -.
DR BioCyc; MetaCyc:EG11529-MON; -.
DR EvolutionaryTrace; P29131; -.
DR PRO; PR:P29131; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0032153; C:cell division site; IC:ComplexPortal.
DR GO; GO:0030428; C:cell septum; IDA:CACAO.
DR GO; GO:0000935; C:division septum; IDA:EcoCyc.
DR GO; GO:1990586; C:divisome complex; IC:ComplexPortal.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0042834; F:peptidoglycan binding; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IDA:CACAO.
DR GO; GO:0000917; P:division septum assembly; IMP:EcoCyc.
DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IC:ComplexPortal.
DR DisProt; DP02271; -.
DR Gene3D; 3.30.70.1070; -; 1.
DR HAMAP; MF_02039; FtsN_entero; 1.
DR InterPro; IPR011930; FtsN.
DR InterPro; IPR007730; SPOR-like_dom.
DR InterPro; IPR036680; SPOR-like_sf.
DR Pfam; PF05036; SPOR; 1.
DR SUPFAM; SSF110997; SSF110997; 1.
DR TIGRFAMs; TIGR02223; ftsN; 1.
DR PROSITE; PS51724; SPOR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cell inner membrane;
KW Cell membrane; Disulfide bond; Membrane; Reference proteome; Repeat;
KW Septation; Transmembrane; Transmembrane helix.
FT CHAIN 1..319
FT /note="Cell division protein FtsN"
FT /id="PRO_0000087376"
FT TOPO_DOM 1..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02039,
FT ECO:0000305|PubMed:8631709"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02039"
FT TOPO_DOM 55..319
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02039,
FT ECO:0000305|PubMed:8631709"
FT REPEAT 115..120
FT /note="1-1"
FT REPEAT 145..150
FT /note="1-2"
FT REPEAT 197..200
FT /note="2-1"
FT REPEAT 220..223
FT /note="2-2"
FT DOMAIN 242..316
FT /note="SPOR"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02039"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4..6
FT /note="Mediates interaction with FtsA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02039,
FT ECO:0000269|PubMed:25496259"
FT REGION 60..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..150
FT /note="2 X 6 AA repeats"
FT REGION 140..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..223
FT /note="2 X 4 AA repeats"
FT COMPBIAS 140..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 252..312
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02039,
FT ECO:0000269|PubMed:24056104"
FT MUTAGEN 5
FT /note="D->N: Causes significant impairment of the
FT interaction with FtsA."
FT /evidence="ECO:0000269|PubMed:25496259"
FT MUTAGEN 83
FT /note="W->L,T: Lack of activity."
FT /evidence="ECO:0000269|PubMed:25496160"
FT MUTAGEN 85
FT /note="Y->S,W: Lack of activity."
FT /evidence="ECO:0000269|PubMed:25496160"
FT MUTAGEN 89
FT /note="L->S: Lack of activity."
FT /evidence="ECO:0000269|PubMed:25496160"
FT MUTAGEN 251
FT /note="Q->A: Reduces septal localization by a factor of at
FT least 3."
FT /evidence="ECO:0000269|PubMed:24056104"
FT MUTAGEN 251
FT /note="Q->E: Severe localization defects. Binds
FT peptidoglycan poorly."
FT /evidence="ECO:0000269|PubMed:24056104"
FT MUTAGEN 252
FT /note="C->A: Severely reduces stability of the protein."
FT /evidence="ECO:0000269|PubMed:24056104"
FT MUTAGEN 254
FT /note="S->A: Reduces septal localization by a factor of at
FT least 3."
FT /evidence="ECO:0000269|PubMed:24056104"
FT MUTAGEN 254
FT /note="S->E: Binds peptidoglycan poorly."
FT /evidence="ECO:0000269|PubMed:24056104"
FT MUTAGEN 263
FT /note="T->D: Intermediate localization defects."
FT /evidence="ECO:0000269|PubMed:24056104"
FT MUTAGEN 270
FT /note="F->A: Intermediate localization defects."
FT /evidence="ECO:0000269|PubMed:24056104"
FT MUTAGEN 283
FT /note="W->A: Reduces septal localization by a factor of at
FT least 3."
FT /evidence="ECO:0000269|PubMed:24056104"
FT MUTAGEN 283
FT /note="W->D: Severe localization defects."
FT /evidence="ECO:0000269|PubMed:24056104"
FT MUTAGEN 285
FT /note="R->A: Reduces septal localization by a factor of at
FT least 3. Binds peptidoglycan poorly."
FT /evidence="ECO:0000269|PubMed:24056104"
FT MUTAGEN 312
FT /note="C->A: Severely reduces stability of the protein."
FT /evidence="ECO:0000269|PubMed:24056104"
FT MUTAGEN 313
FT /note="I->A: Reduces septal localization by a factor of at
FT least 3."
FT /evidence="ECO:0000269|PubMed:24056104"
FT CONFLICT 29
FT /note="L -> V (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT HELIX 80..90
FT /evidence="ECO:0007829|PDB:6YN0"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:1UTA"
FT HELIX 258..271
FT /evidence="ECO:0007829|PDB:1UTA"
FT STRAND 275..279
FT /evidence="ECO:0007829|PDB:1UTA"
FT STRAND 281..290
FT /evidence="ECO:0007829|PDB:1UTA"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:1UTA"
FT HELIX 296..307
FT /evidence="ECO:0007829|PDB:1UTA"
SQ SEQUENCE 319 AA; 35793 MW; 21CEA5771FF3FB66 CRC64;
MAQRDYVRRS QPAPSRRKKS TSRKKQRNLP AVSPAMVAIA AAVLVTFIGG LYFITHHKKE
ESETLQSQKV TGNGLPPKPE ERWRYIKELE SRQPGVRAPT EPSAGGEVKT PEQLTPEQRQ
LLEQMQADMR QQPTQLVEVP WNEQTPEQRQ QTLQRQRQAQ QLAEQQRLAQ QSRTTEQSWQ
QQTRTSQAAP VQAQPRQSKP ASSQQPYQDL LQTPAHTTAQ SKPQQAAPVA RAADAPKPTA
EKKDERRWMV QCGSFRGAEQ AETVRAQLAF EGFDSKITTN NGWNRVVIGP VKGKENADST
LNRLKMAGHT NCIRLAAGG
