SECA_BACSU
ID SECA_BACSU Reviewed; 841 AA.
AC P28366;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Protein translocase subunit SecA {ECO:0000255|HAMAP-Rule:MF_01382};
DE EC=7.4.2.8 {ECO:0000255|HAMAP-Rule:MF_01382, ECO:0000305|PubMed:8440733};
GN Name=secA {ECO:0000255|HAMAP-Rule:MF_01382}; Synonyms=div+;
GN OrderedLocusNames=BSU35300;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=1901557; DOI=10.1016/0378-1119(91)90110-w;
RA Sadaie Y., Takamatsu H., Nakamura K., Yamane K.;
RT "Sequencing reveals similarity of the wild-type div+ gene of Bacillus
RT subtilis to the Escherichia coli secA gene.";
RL Gene 98:101-105(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969505; DOI=10.1099/13500872-142-11-3079;
RA Soldo B., Lazarevic V., Mauel C., Karamata D.;
RT "Sequence of the 305 degrees-307 degrees region of the Bacillus subtilis
RT chromosome.";
RL Microbiology 142:3079-3088(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-364.
RX PubMed=1832735; DOI=10.1007/bf00260635;
RA Overhoff B., Klein M., Spies M., Freudl R.;
RT "Identification of a gene fragment which codes for the 364 amino-terminal
RT amino acid residues of a SecA homologue from Bacillus subtilis: further
RT evidence for the conservation of the protein export apparatus in Gram-
RT positive and Gram-negative bacteria.";
RL Mol. Gen. Genet. 228:417-423(1991).
RN [5]
RP CATALYTIC ACTIVITY, AND MUTAGENESIS OF LYS-101 AND LYS-106.
RX PubMed=8440733; DOI=10.1016/s0021-9258(18)53638-3;
RA Klose M., Schimz K.L., van der Wolk J., Driessen A.J., Freudl R.;
RT "Lysine 106 of the putative catalytic ATP-binding site of the Bacillus
RT subtilis SecA protein is required for functional complementation of
RT Escherichia coli secA mutants in vivo.";
RL J. Biol. Chem. 268:4504-4510(1993).
RN [6]
RP SUBCELLULAR LOCATION.
RC STRAIN=168 / PY79;
RX PubMed=27362352; DOI=10.1371/journal.pgen.1006116;
RA Dempwolff F., Schmidt F.K., Hervas A.B., Stroh A., Roesch T.C., Riese C.N.,
RA Dersch S., Heimerl T., Lucena D., Huelsbusch N., Stuermer C.A.,
RA Takeshita N., Fischer R., Eckhardt B., Graumann P.L.;
RT "Super Resolution Fluorescence Microscopy and Tracking of Bacterial
RT Flotillin (Reggie) Paralogs Provide Evidence for Defined-Sized Protein
RT Microdomains within the Bacterial Membrane but Absence of Clusters
RT Containing Detergent-Resistant Proteins.";
RL PLoS Genet. 12:e1006116-e1006116(2016).
RN [7] {ECO:0007744|PDB:1M6N, ECO:0007744|PDB:1M74}
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-802 (MONOMERIC AND DIMERIC) WITH
RP AND WITHOUT BOUND ADP.
RX PubMed=12242434; DOI=10.1126/science.1074424;
RA Hunt J.F., Weinkauf S., Henry L., Fak J.J., McNicholas P., Oliver D.B.,
RA Deisenhofer J.;
RT "Nucleotide control of interdomain interactions in the conformational
RT reaction cycle of SecA.";
RL Science 297:2018-2026(2002).
RN [8] {ECO:0007744|PDB:1TF2, ECO:0007744|PDB:1TF5}
RP X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) OF OPEN MONOMERIC SECA IN COMPLEX
RP WITH ADP.
RX PubMed=15256599; DOI=10.1073/pnas.0401742101;
RA Osborne A.R., Clemons W.M. Jr., Rapoport T.A.;
RT "A large conformational change of the translocation ATPase SecA.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:10937-10942(2004).
RN [9] {ECO:0007744|PDB:2IBM}
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 1-780 IN A DIMERIC FORM IN COMPLEX
RP WITH ADP, STUDY OF DIMERIC FORMS, AND MUTAGENESIS OF GLY-587; ASN-588 AND
RP ARG-750.
RX PubMed=16989859; DOI=10.1016/j.jmb.2006.08.044;
RA Zimmer J., Li W., Rapoport T.A.;
RT "A novel dimer interface and conformational changes revealed by an X-ray
RT structure of B. subtilis SecA.";
RL J. Mol. Biol. 364:259-265(2006).
RN [10] {ECO:0007744|PDB:3DL8}
RP X-RAY CRYSTALLOGRAPHY (7.5 ANGSTROMS) OF 1-779 IN COMPLEX WITH SECYEG FROM
RP A.AEOLICUS.
RX PubMed=18923516; DOI=10.1038/nature07335;
RA Zimmer J., Nam Y., Rapoport T.A.;
RT "Structure of a complex of the ATPase SecA and the protein-translocation
RT channel.";
RL Nature 455:936-943(2008).
RN [11] {ECO:0007744|PDB:3JV2}
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-780 IN COMPLEX WITH ADP.
RX PubMed=19850053; DOI=10.1016/j.jmb.2009.10.024;
RA Zimmer J., Rapoport T.A.;
RT "Conformational flexibility and peptide interaction of the translocation
RT ATPase SecA.";
RL J. Mol. Biol. 394:606-612(2009).
CC -!- FUNCTION: Part of the Sec protein translocase complex. Interacts with
CC the SecYEG preprotein conducting channel. Has a central role in
CC coupling the hydrolysis of ATP to the transfer of proteins into and
CC across the cell membrane, serving as an ATP-driven molecular motor
CC driving the stepwise translocation of polypeptide chains across the
CC membrane. {ECO:0000255|HAMAP-Rule:MF_01382}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + cellular proteinSide 1 = ADP + phosphate +
CC cellular proteinSide 2.; EC=7.4.2.8; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01382, ECO:0000305|PubMed:8440733};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01382};
CC Note=May bind 1 zinc ion per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01382};
CC -!- SUBUNIT: Part of the essential Sec protein translocation apparatus
CC which comprises SecA, SecYEG and auxiliary proteins SecDF. Other
CC proteins may be involved. Monomer and many different homodimers can be
CC isolated (PubMed:16989859), some of which are not formed in the
CC presence of a synthetic signal peptide. A single SecA monomer interacts
CC with SecY in the channel. Only shows some colocalization with FloA or
CC FloT membrane assemblies (PubMed:27362352).
CC {ECO:0000269|PubMed:16989859, ECO:0000269|PubMed:18923516,
CC ECO:0000269|PubMed:27362352}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01382,
CC ECO:0000269|PubMed:27362352}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01382}; Cytoplasmic side {ECO:0000255|HAMAP-
CC Rule:MF_01382}. Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01382}. Membrane
CC raft {ECO:0000269|PubMed:27362352}. Note=Distribution is 50-50.
CC {ECO:0000255|HAMAP-Rule:MF_01382}.
CC -!- SIMILARITY: Belongs to the SecA family. {ECO:0000255|HAMAP-
CC Rule:MF_01382}.
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DR EMBL; D10279; BAA01122.1; -; Genomic_DNA.
DR EMBL; U56901; AAC44957.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15547.1; -; Genomic_DNA.
DR EMBL; X62035; CAA43977.1; -; Genomic_DNA.
DR PIR; JQ0647; JQ0647.
DR RefSeq; NP_391410.1; NC_000964.3.
DR RefSeq; WP_003228033.1; NZ_JNCM01000033.1.
DR PDB; 1M6N; X-ray; 2.70 A; A=1-802.
DR PDB; 1M74; X-ray; 3.00 A; A=1-802.
DR PDB; 1TF2; X-ray; 2.90 A; A=1-841.
DR PDB; 1TF5; X-ray; 2.18 A; A=1-841.
DR PDB; 2IBM; X-ray; 3.20 A; A/B=1-780.
DR PDB; 3DL8; X-ray; 7.50 A; A/B=1-779.
DR PDB; 3IQM; X-ray; 3.40 A; A=1-802.
DR PDB; 3IQY; X-ray; 3.30 A; A=1-841.
DR PDB; 3JV2; X-ray; 2.50 A; A/B=1-780.
DR PDB; 5EUL; X-ray; 3.70 A; A=1-780.
DR PDB; 6ITC; EM; 3.45 A; A=1-780.
DR PDBsum; 1M6N; -.
DR PDBsum; 1M74; -.
DR PDBsum; 1TF2; -.
DR PDBsum; 1TF5; -.
DR PDBsum; 2IBM; -.
DR PDBsum; 3DL8; -.
DR PDBsum; 3IQM; -.
DR PDBsum; 3IQY; -.
DR PDBsum; 3JV2; -.
DR PDBsum; 5EUL; -.
DR PDBsum; 6ITC; -.
DR AlphaFoldDB; P28366; -.
DR SMR; P28366; -.
DR DIP; DIP-59805N; -.
DR IntAct; P28366; 7.
DR MINT; P28366; -.
DR STRING; 224308.BSU35300; -.
DR TCDB; 3.A.5.2.1; the general secretory pathway (sec) family.
DR jPOST; P28366; -.
DR PaxDb; P28366; -.
DR PRIDE; P28366; -.
DR EnsemblBacteria; CAB15547; CAB15547; BSU_35300.
DR GeneID; 936711; -.
DR KEGG; bsu:BSU35300; -.
DR PATRIC; fig|224308.179.peg.3820; -.
DR eggNOG; COG0653; Bacteria.
DR InParanoid; P28366; -.
DR OMA; MVHYDVQ; -.
DR PhylomeDB; P28366; -.
DR BioCyc; BSUB:BSU35300-MON; -.
DR BRENDA; 7.4.2.5; 658.
DR EvolutionaryTrace; P28366; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0031522; C:cell envelope Sec protein transport complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0015462; F:ABC-type protein transporter activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008564; F:protein-exporting ATPase activity; IEA:UniProtKB-EC.
DR GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:UniProtKB-UniRule.
DR GO; GO:0017038; P:protein import; IEA:InterPro.
DR GO; GO:0006605; P:protein targeting; IEA:UniProtKB-UniRule.
DR GO; GO:0043952; P:protein transport by the Sec complex; IBA:GO_Central.
DR CDD; cd18803; SF2_C_secA; 1.
DR Gene3D; 3.40.50.300; -; 3.
DR HAMAP; MF_01382; SecA; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004027; SEC_C_motif.
DR InterPro; IPR000185; SecA.
DR InterPro; IPR020937; SecA_CS.
DR InterPro; IPR011115; SecA_DEAD.
DR InterPro; IPR014018; SecA_motor_DEAD.
DR InterPro; IPR011130; SecA_preprotein_X-link_dom.
DR InterPro; IPR044722; SecA_SF2_C.
DR InterPro; IPR011116; SecA_Wing/Scaffold.
DR InterPro; IPR036266; SecA_Wing/Scaffold_sf.
DR InterPro; IPR036670; SecA_X-link_sf.
DR PANTHER; PTHR30612; PTHR30612; 1.
DR Pfam; PF02810; SEC-C; 1.
DR Pfam; PF07517; SecA_DEAD; 1.
DR Pfam; PF01043; SecA_PP_bind; 1.
DR Pfam; PF07516; SecA_SW; 1.
DR PRINTS; PR00906; SECA.
DR SMART; SM00957; SecA_DEAD; 1.
DR SMART; SM00958; SecA_PP_bind; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF81767; SSF81767; 1.
DR SUPFAM; SSF81886; SSF81886; 1.
DR TIGRFAMs; TIGR00963; secA; 1.
DR PROSITE; PS01312; SECA; 1.
DR PROSITE; PS51196; SECA_MOTOR_DEAD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Cytoplasm; Membrane;
KW Metal-binding; Nucleotide-binding; Protein transport; Reference proteome;
KW Translocase; Translocation; Transport; Zinc.
FT CHAIN 1..841
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000109576"
FT REGION 786..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 79..80
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15256599,
FT ECO:0000269|PubMed:19850053, ECO:0007744|PDB:1TF2,
FT ECO:0007744|PDB:3JV2"
FT BINDING 85
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382,
FT ECO:0000269|PubMed:12242434, ECO:0000269|PubMed:15256599,
FT ECO:0000269|PubMed:16989859, ECO:0000269|PubMed:19850053,
FT ECO:0007744|PDB:1M74, ECO:0007744|PDB:1TF2,
FT ECO:0007744|PDB:2IBM, ECO:0007744|PDB:3JV2"
FT BINDING 103..107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382,
FT ECO:0000269|PubMed:12242434, ECO:0000269|PubMed:15256599,
FT ECO:0000269|PubMed:16989859, ECO:0000269|PubMed:19850053,
FT ECO:0007744|PDB:1M74, ECO:0007744|PDB:1TF2,
FT ECO:0007744|PDB:2IBM, ECO:0007744|PDB:3JV2"
FT BINDING 492
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382,
FT ECO:0000269|PubMed:12242434, ECO:0000269|PubMed:15256599,
FT ECO:0000269|PubMed:16989859, ECO:0007744|PDB:1M74,
FT ECO:0007744|PDB:1TF2, ECO:0007744|PDB:2IBM"
FT BINDING 825
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 827
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 836
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 837
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT MUTAGEN 101
FT /note="K->N: Can restore growth of E.coli secA mutants."
FT /evidence="ECO:0000269|PubMed:8440733"
FT MUTAGEN 106
FT /note="K->N: Loss of activity. Cannot complement E.coli
FT secA mutants."
FT /evidence="ECO:0000269|PubMed:8440733"
FT MUTAGEN 587
FT /note="G->C: Forms position 587-750 dimers upon oxidation
FT in vitro; when associated with C-750. Does not form
FT position 587-587 dimers (homodimers)."
FT /evidence="ECO:0000269|PubMed:16989859"
FT MUTAGEN 588
FT /note="N->C: Forms position 588-588 dimers upon oxidation
FT in vitro (homodimers)."
FT /evidence="ECO:0000269|PubMed:16989859"
FT MUTAGEN 750
FT /note="R->C: Forms position 587-750 dimers upon oxidation
FT in vitro; when associated with C-587. Also forms position
FT 750-750 dimers (homodimers)."
FT /evidence="ECO:0000269|PubMed:16989859"
FT CONFLICT 126
FT /note="V -> I (in Ref. 4; CAA43977)"
FT /evidence="ECO:0000305"
FT HELIX 1..6
FT /evidence="ECO:0007829|PDB:1TF5"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:2IBM"
FT HELIX 18..28
FT /evidence="ECO:0007829|PDB:1TF5"
FT HELIX 31..34
FT /evidence="ECO:0007829|PDB:1TF5"
FT HELIX 38..53
FT /evidence="ECO:0007829|PDB:1TF5"
FT HELIX 58..77
FT /evidence="ECO:0007829|PDB:1TF5"
FT HELIX 83..93
FT /evidence="ECO:0007829|PDB:1TF5"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:1TF5"
FT HELIX 106..118
FT /evidence="ECO:0007829|PDB:1TF5"
FT TURN 119..122
FT /evidence="ECO:0007829|PDB:1M6N"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:1TF5"
FT HELIX 131..147
FT /evidence="ECO:0007829|PDB:1TF5"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:1TF5"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:2IBM"
FT HELIX 161..169
FT /evidence="ECO:0007829|PDB:1TF5"
FT STRAND 170..176
FT /evidence="ECO:0007829|PDB:1TF5"
FT HELIX 177..187
FT /evidence="ECO:0007829|PDB:1TF5"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:1TF5"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:1TF5"
FT HELIX 209..213
FT /evidence="ECO:0007829|PDB:1TF5"
FT TURN 214..218
FT /evidence="ECO:0007829|PDB:1TF5"
FT STRAND 220..228
FT /evidence="ECO:0007829|PDB:1TF5"
FT HELIX 232..241
FT /evidence="ECO:0007829|PDB:1TF5"
FT TURN 242..244
FT /evidence="ECO:0007829|PDB:3IQM"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:1TF5"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:1TF5"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:3JV2"
FT HELIX 263..272
FT /evidence="ECO:0007829|PDB:1TF5"
FT TURN 275..277
FT /evidence="ECO:0007829|PDB:1M6N"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:1TF2"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:1TF5"
FT HELIX 284..298
FT /evidence="ECO:0007829|PDB:1TF5"
FT TURN 302..304
FT /evidence="ECO:0007829|PDB:1TF5"
FT STRAND 305..309
FT /evidence="ECO:0007829|PDB:1TF5"
FT STRAND 312..316
FT /evidence="ECO:0007829|PDB:1TF5"
FT TURN 318..320
FT /evidence="ECO:0007829|PDB:1TF5"
FT STRAND 325..329
FT /evidence="ECO:0007829|PDB:6ITC"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:1M6N"
FT HELIX 333..340
FT /evidence="ECO:0007829|PDB:1TF5"
FT STRAND 349..356
FT /evidence="ECO:0007829|PDB:1TF5"
FT HELIX 357..361
FT /evidence="ECO:0007829|PDB:1TF5"
FT STRAND 364..372
FT /evidence="ECO:0007829|PDB:1TF5"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:1TF5"
FT HELIX 378..385
FT /evidence="ECO:0007829|PDB:1TF5"
FT STRAND 389..391
FT /evidence="ECO:0007829|PDB:1TF5"
FT STRAND 399..402
FT /evidence="ECO:0007829|PDB:3IQY"
FT STRAND 406..410
FT /evidence="ECO:0007829|PDB:1TF5"
FT HELIX 411..427
FT /evidence="ECO:0007829|PDB:1TF5"
FT STRAND 432..437
FT /evidence="ECO:0007829|PDB:1TF5"
FT HELIX 439..450
FT /evidence="ECO:0007829|PDB:1TF5"
FT TURN 451..453
FT /evidence="ECO:0007829|PDB:1TF5"
FT STRAND 457..459
FT /evidence="ECO:0007829|PDB:1TF5"
FT STRAND 461..463
FT /evidence="ECO:0007829|PDB:1M6N"
FT HELIX 464..471
FT /evidence="ECO:0007829|PDB:1TF5"
FT TURN 472..475
FT /evidence="ECO:0007829|PDB:1TF5"
FT STRAND 480..484
FT /evidence="ECO:0007829|PDB:1TF5"
FT TURN 485..490
FT /evidence="ECO:0007829|PDB:3JV2"
FT TURN 497..499
FT /evidence="ECO:0007829|PDB:3JV2"
FT HELIX 500..502
FT /evidence="ECO:0007829|PDB:1TF5"
FT STRAND 504..511
FT /evidence="ECO:0007829|PDB:1TF5"
FT HELIX 516..523
FT /evidence="ECO:0007829|PDB:1TF5"
FT HELIX 528..530
FT /evidence="ECO:0007829|PDB:1TF5"
FT STRAND 533..540
FT /evidence="ECO:0007829|PDB:1TF5"
FT STRAND 541..543
FT /evidence="ECO:0007829|PDB:6ITC"
FT HELIX 545..547
FT /evidence="ECO:0007829|PDB:1TF5"
FT HELIX 550..561
FT /evidence="ECO:0007829|PDB:1TF5"
FT STRAND 565..567
FT /evidence="ECO:0007829|PDB:1TF5"
FT HELIX 572..618
FT /evidence="ECO:0007829|PDB:1TF5"
FT STRAND 621..623
FT /evidence="ECO:0007829|PDB:2IBM"
FT HELIX 624..641
FT /evidence="ECO:0007829|PDB:1TF5"
FT STRAND 645..648
FT /evidence="ECO:0007829|PDB:3IQY"
FT HELIX 649..651
FT /evidence="ECO:0007829|PDB:1M6N"
FT HELIX 657..662
FT /evidence="ECO:0007829|PDB:1TF5"
FT TURN 663..665
FT /evidence="ECO:0007829|PDB:1TF5"
FT STRAND 668..671
FT /evidence="ECO:0007829|PDB:1M6N"
FT STRAND 672..675
FT /evidence="ECO:0007829|PDB:1TF5"
FT HELIX 681..702
FT /evidence="ECO:0007829|PDB:1TF5"
FT TURN 704..706
FT /evidence="ECO:0007829|PDB:2IBM"
FT HELIX 707..736
FT /evidence="ECO:0007829|PDB:1TF5"
FT HELIX 738..740
FT /evidence="ECO:0007829|PDB:1TF5"
FT STRAND 744..746
FT /evidence="ECO:0007829|PDB:1TF5"
FT HELIX 748..776
FT /evidence="ECO:0007829|PDB:1TF5"
FT STRAND 794..797
FT /evidence="ECO:0007829|PDB:1M6N"
SQ SEQUENCE 841 AA; 95531 MW; 9AAC3630139F5EFF CRC64;
MLGILNKMFD PTKRTLNRYE KIANDIDAIR GDYENLSDDA LKHKTIEFKE RLEKGATTDD
LLVEAFAVVR EASRRVTGMF PFKVQLMGGV ALHDGNIAEM KTGEGKTLTS TLPVYLNALT
GKGVHVVTVN EYLASRDAEQ MGKIFEFLGL TVGLNLNSMS KDEKREAYAA DITYSTNNEL
GFDYLRDNMV LYKEQMVQRP LHFAVIDEVD SILIDEARTP LIISGQAAKS TKLYVQANAF
VRTLKAEKDY TYDIKTKAVQ LTEEGMTKAE KAFGIDNLFD VKHVALNHHI NQALKAHVAM
QKDVDYVVED GQVVIVDSFT GRLMKGRRYS EGLHQAIEAK EGLEIQNESM TLATITFQNY
FRMYEKLAGM TGTAKTEEEE FRNIYNMQVV TIPTNRPVVR DDRPDLIYRT MEGKFKAVAE
DVAQRYMTGQ PVLVGTVAVE TSELISKLLK NKGIPHQVLN AKNHEREAQI IEEAGQKGAV
TIATNMAGRG TDIKLGEGVK ELGGLAVVGT ERHESRRIDN QLRGRSGRQG DPGITQFYLS
MEDELMRRFG AERTMAMLDR FGMDDSTPIQ SKMVSRAVES SQKRVEGNNF DSRKQLLQYD
DVLRQQREVI YKQRFEVIDS ENLREIVENM IKSSLERAIA AYTPREELPE EWKLDGLVDL
INTTYLDEGA LEKSDIFGKE PDEMLELIMD RIITKYNEKE EQFGKEQMRE FEKVIVLRAV
DSKWMDHIDA MDQLRQGIHL RAYAQTNPLR EYQMEGFAMF EHMIESIEDE VAKFVMKAEI
ENNLEREEVV QGQTTAHQPQ EGDDNKKAKK APVRKVVDIG RNAPCHCGSG KKYKNCCGRT
E
