PKSJ_BACSU
ID PKSJ_BACSU Reviewed; 5043 AA.
AC P40806; P40803;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 3.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Polyketide synthase PksJ;
DE Short=PKS;
GN Name=pksJ; Synonyms=pksK; OrderedLocusNames=BSU17180;
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 / PB1424;
RX PubMed=7704258; DOI=10.1099/13500872-141-2-299;
RA Albertini A.M., Caramori T., Scoffone F., Scotti C., Galizzi A.;
RT "Sequence around the 159 degree region of the Bacillus subtilis genome: the
RT pksX locus spans 33.6 kb.";
RL Microbiology 141:299-309(1995).
RN [2]
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 [3]
RP SEQUENCE REVISION.
RX PubMed=10568751; DOI=10.1101/gr.9.11.1116;
RA Medigue C., Rose M., Viari A., Danchin A.;
RT "Detecting and analyzing DNA sequencing errors: toward a higher quality of
RT the Bacillus subtilis genome sequence.";
RL Genome Res. 9:1116-1127(1999).
RN [4]
RP SEQUENCE REVISION TO 87; 619 AND 4981.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [5]
RP FUNCTION AS AN ACYL CARRIER PROTEIN, AND PHOSPHOPANTETHEINYLATION AT
RP SER-1689.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=16460000; DOI=10.1021/bi052333k;
RA Dorrestein P.C., Blackhall J., Straight P.D., Fischbach M.A.,
RA Garneau-Tsodikova S., Edwards D.J., McLaughlin S., Lin M., Gerwick W.H.,
RA Kolter R., Walsh C.T., Kelleher N.L.;
RT "Activity screening of carrier domains within nonribosomal peptide
RT synthetases using complex substrate mixtures and large molecule mass
RT spectrometry.";
RL Biochemistry 45:1537-1546(2006).
RN [6]
RP SUBCELLULAR LOCATION.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=17190806; DOI=10.1073/pnas.0609073103;
RA Straight P.D., Fischbach M.A., Walsh C.T., Rudner D.Z., Kolter R.;
RT "A singular enzymatic megacomplex from Bacillus subtilis.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:305-310(2007).
RN [7]
RP FUNCTION IN BACILLAENE BIOSYNTHESIS.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=17234808; DOI=10.1073/pnas.0610503104;
RA Butcher R.A., Schroeder F.C., Fischbach M.A., Straight P.D., Kolter R.,
RA Walsh C.T., Clardy J.;
RT "The identification of bacillaene, the product of the PksX megacomplex in
RT Bacillus subtilis.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1506-1509(2007).
CC -!- FUNCTION: Involved in some intermediate steps for the synthesis of the
CC antibiotic polyketide bacillaene which is involved in secondary
CC metabolism. {ECO:0000269|PubMed:16460000, ECO:0000269|PubMed:17234808}.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000305};
CC Note=Binds 5 phosphopantetheines covalently. {ECO:0000305};
CC -!- PATHWAY: Antibiotic biosynthesis; bacillaene biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17190806}.
CC -!- MISCELLANEOUS: The acyl carrier 2 domain binds glycine.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be two separate ORFs named pksJ and
CC pksK. {ECO:0000305}.
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DR EMBL; U11039; AAA85143.1; ALT_SEQ; Genomic_DNA.
DR EMBL; U11039; AAA85144.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL009126; CAB13589.3; -; Genomic_DNA.
DR PIR; A69679; A69679.
DR PIR; H69678; H69678.
DR RefSeq; NP_389598.3; NC_000964.3.
DR RefSeq; WP_003245563.1; NZ_JNCM01000035.1.
DR PDB; 4J1Q; X-ray; 2.35 A; A=2669-3111.
DR PDB; 4J1S; X-ray; 3.01 A; A=2669-3111.
DR PDB; 4NA1; X-ray; 1.95 A; A/B=3336-3951.
DR PDB; 4NA2; X-ray; 2.30 A; A/B=3336-3951.
DR PDB; 4NA3; X-ray; 2.89 A; A/B=3336-3951.
DR PDB; 5KTK; X-ray; 1.98 A; A=3954-4472.
DR PDBsum; 4J1Q; -.
DR PDBsum; 4J1S; -.
DR PDBsum; 4NA1; -.
DR PDBsum; 4NA2; -.
DR PDBsum; 4NA3; -.
DR PDBsum; 5KTK; -.
DR SMR; P40806; -.
DR DIP; DIP-60662N; -.
DR IntAct; P40806; 7.
DR STRING; 224308.BSU17180; -.
DR PaxDb; P40806; -.
DR PRIDE; P40806; -.
DR EnsemblBacteria; CAB13589; CAB13589; BSU_17180.
DR GeneID; 940043; -.
DR KEGG; bsu:BSU17180; -.
DR PATRIC; fig|224308.179.peg.1863; -.
DR eggNOG; COG0300; Bacteria.
DR eggNOG; COG0318; Bacteria.
DR eggNOG; COG1020; Bacteria.
DR eggNOG; COG1028; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR InParanoid; P40806; -.
DR OMA; LFFEHET; -.
DR PhylomeDB; P40806; -.
DR BioCyc; BSUB:BSU17180-MON; -.
DR UniPathway; UPA01003; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0004312; F:fatty acid synthase activity; IBA:GO_Central.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0071770; P:DIM/DIP cell wall layer assembly; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR Gene3D; 1.10.1200.10; -; 5.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.30.300.30; -; 2.
DR Gene3D; 3.30.559.10; -; 1.
DR Gene3D; 3.40.47.10; -; 3.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020807; PKS_dehydratase.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF00501; AMP-binding; 2.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 2.
DR Pfam; PF00109; ketoacyl-synt; 3.
DR Pfam; PF02801; Ketoacyl-synt_C; 3.
DR Pfam; PF08659; KR; 2.
DR Pfam; PF00550; PP-binding; 5.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00825; PKS_KS; 3.
DR SMART; SM00823; PKS_PP; 5.
DR SUPFAM; SSF47336; SSF47336; 5.
DR SUPFAM; SSF51735; SSF51735; 3.
DR SUPFAM; SSF53901; SSF53901; 3.
DR TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR PROSITE; PS00455; AMP_BINDING; 2.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 2.
DR PROSITE; PS50075; CARRIER; 5.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Antibiotic biosynthesis; Coiled coil;
KW Cytoplasm; Ligase; Multifunctional enzyme; NADP; Phosphopantetheine;
KW Phosphoprotein; Reference proteome; Repeat; Transferase.
FT CHAIN 1..5043
FT /note="Polyketide synthase PksJ"
FT /id="PRO_0000193184"
FT DOMAIN 590..667
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 1654..1729
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 3114..3188
FT /note="Carrier 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 3212..3286
FT /note="Carrier 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 4459..4536
FT /note="Carrier 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 141..481
FT /note="Adenylation 1"
FT REGION 690..989
FT /note="Condensation"
FT /evidence="ECO:0000250"
FT REGION 1181..1578
FT /note="Adenylation 2"
FT /evidence="ECO:0000250"
FT REGION 1763..2189
FT /note="Beta-ketoacyl synthase 1"
FT /evidence="ECO:0000250"
FT REGION 3291..3314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3342..3782
FT /note="Beta-ketoacyl synthase 2"
FT /evidence="ECO:0000250"
FT REGION 4591..4995
FT /note="Beta-ketoacyl synthase 3"
FT /evidence="ECO:0000250"
FT COILED 3839..3872
FT /evidence="ECO:0000255"
FT ACT_SITE 1932
FT /note="For beta-ketoacyl synthase 1 activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 3511
FT /note="For beta-ketoacyl synthase 2 activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 4743
FT /note="For beta-ketoacyl synthase 3 activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 627
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1689
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000269|PubMed:16460000"
FT MOD_RES 3148
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 3246
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 4496
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT CONFLICT 87
FT /note="V -> W (in Ref. 1; AAA85143)"
FT /evidence="ECO:0000305"
FT CONFLICT 619
FT /note="N -> NAN (in Ref. 1; AAA85144)"
FT /evidence="ECO:0000305"
FT CONFLICT 4981
FT /note="D -> G (in Ref. 1; AAA85144)"
FT /evidence="ECO:0000305"
FT STRAND 2669..2678
FT /evidence="ECO:0007829|PDB:4J1Q"
FT STRAND 2692..2700
FT /evidence="ECO:0007829|PDB:4J1Q"
FT HELIX 2703..2712
FT /evidence="ECO:0007829|PDB:4J1Q"
FT TURN 2713..2715
FT /evidence="ECO:0007829|PDB:4J1Q"
FT STRAND 2716..2721
FT /evidence="ECO:0007829|PDB:4J1Q"
FT HELIX 2728..2745
FT /evidence="ECO:0007829|PDB:4J1Q"
FT HELIX 2747..2752
FT /evidence="ECO:0007829|PDB:4J1Q"
FT STRAND 2755..2762
FT /evidence="ECO:0007829|PDB:4J1Q"
FT HELIX 2767..2772
FT /evidence="ECO:0007829|PDB:4J1Q"
FT HELIX 2773..2783
FT /evidence="ECO:0007829|PDB:4J1Q"
FT STRAND 2787..2796
FT /evidence="ECO:0007829|PDB:4J1Q"
FT TURN 2797..2799
FT /evidence="ECO:0007829|PDB:4J1Q"
FT HELIX 2803..2811
FT /evidence="ECO:0007829|PDB:4J1Q"
FT STRAND 2818..2822
FT /evidence="ECO:0007829|PDB:4J1Q"
FT STRAND 2825..2833
FT /evidence="ECO:0007829|PDB:4J1Q"
FT STRAND 2848..2855
FT /evidence="ECO:0007829|PDB:4J1Q"
FT TURN 2856..2858
FT /evidence="ECO:0007829|PDB:4J1Q"
FT HELIX 2860..2873
FT /evidence="ECO:0007829|PDB:4J1Q"
FT STRAND 2877..2881
FT /evidence="ECO:0007829|PDB:4J1Q"
FT HELIX 2888..2899
FT /evidence="ECO:0007829|PDB:4J1Q"
FT STRAND 2903..2906
FT /evidence="ECO:0007829|PDB:4J1Q"
FT HELIX 2914..2927
FT /evidence="ECO:0007829|PDB:4J1Q"
FT STRAND 2933..2936
FT /evidence="ECO:0007829|PDB:4J1Q"
FT TURN 2946..2948
FT /evidence="ECO:0007829|PDB:4J1Q"
FT HELIX 2951..2958
FT /evidence="ECO:0007829|PDB:4J1Q"
FT TURN 2959..2962
FT /evidence="ECO:0007829|PDB:4J1Q"
FT HELIX 2963..2971
FT /evidence="ECO:0007829|PDB:4J1Q"
FT TURN 2972..2974
FT /evidence="ECO:0007829|PDB:4J1Q"
FT STRAND 2978..2985
FT /evidence="ECO:0007829|PDB:4J1Q"
FT HELIX 2986..2990
FT /evidence="ECO:0007829|PDB:4J1Q"
FT HELIX 2996..3017
FT /evidence="ECO:0007829|PDB:4J1Q"
FT STRAND 3023..3030
FT /evidence="ECO:0007829|PDB:4J1Q"
FT HELIX 3044..3052
FT /evidence="ECO:0007829|PDB:4J1Q"
FT HELIX 3059..3072
FT /evidence="ECO:0007829|PDB:4J1Q"
FT STRAND 3075..3082
FT /evidence="ECO:0007829|PDB:4J1Q"
FT HELIX 3084..3091
FT /evidence="ECO:0007829|PDB:4J1Q"
FT STRAND 3342..3351
FT /evidence="ECO:0007829|PDB:4NA1"
FT STRAND 3354..3356
FT /evidence="ECO:0007829|PDB:4NA1"
FT HELIX 3357..3365
FT /evidence="ECO:0007829|PDB:4NA1"
FT TURN 3376..3378
FT /evidence="ECO:0007829|PDB:4NA1"
FT HELIX 3381..3384
FT /evidence="ECO:0007829|PDB:4NA1"
FT TURN 3388..3390
FT /evidence="ECO:0007829|PDB:4NA1"
FT STRAND 3399..3401
FT /evidence="ECO:0007829|PDB:4NA1"
FT STRAND 3406..3409
FT /evidence="ECO:0007829|PDB:4NA2"
FT HELIX 3411..3414
FT /evidence="ECO:0007829|PDB:4NA1"
FT HELIX 3418..3421
FT /evidence="ECO:0007829|PDB:4NA1"
FT HELIX 3426..3442
FT /evidence="ECO:0007829|PDB:4NA1"
FT HELIX 3446..3449
FT /evidence="ECO:0007829|PDB:4NA1"
FT STRAND 3455..3459
FT /evidence="ECO:0007829|PDB:4NA1"
FT HELIX 3465..3471
FT /evidence="ECO:0007829|PDB:4NA1"
FT HELIX 3480..3484
FT /evidence="ECO:0007829|PDB:4NA1"
FT HELIX 3489..3498
FT /evidence="ECO:0007829|PDB:4NA1"
FT STRAND 3504..3507
FT /evidence="ECO:0007829|PDB:4NA1"
FT HELIX 3510..3512
FT /evidence="ECO:0007829|PDB:4NA1"
FT HELIX 3513..3526
FT /evidence="ECO:0007829|PDB:4NA1"
FT STRAND 3531..3539
FT /evidence="ECO:0007829|PDB:4NA1"
FT HELIX 3545..3552
FT /evidence="ECO:0007829|PDB:4NA1"
FT STRAND 3577..3585
FT /evidence="ECO:0007829|PDB:4NA1"
FT HELIX 3586..3592
FT /evidence="ECO:0007829|PDB:4NA1"
FT STRAND 3597..3607
FT /evidence="ECO:0007829|PDB:4NA1"
FT HELIX 3619..3633
FT /evidence="ECO:0007829|PDB:4NA1"
FT HELIX 3637..3639
FT /evidence="ECO:0007829|PDB:4NA1"
FT STRAND 3642..3644
FT /evidence="ECO:0007829|PDB:4NA1"
FT HELIX 3653..3669
FT /evidence="ECO:0007829|PDB:4NA1"
FT STRAND 3679..3681
FT /evidence="ECO:0007829|PDB:4NA2"
FT STRAND 3684..3687
FT /evidence="ECO:0007829|PDB:4NA1"
FT HELIX 3690..3693
FT /evidence="ECO:0007829|PDB:4NA1"
FT HELIX 3697..3699
FT /evidence="ECO:0007829|PDB:4NA1"
FT HELIX 3700..3713
FT /evidence="ECO:0007829|PDB:4NA1"
FT STRAND 3724..3726
FT /evidence="ECO:0007829|PDB:4NA1"
FT STRAND 3735..3739
FT /evidence="ECO:0007829|PDB:4NA1"
FT STRAND 3752..3754
FT /evidence="ECO:0007829|PDB:4NA1"
FT STRAND 3760..3766
FT /evidence="ECO:0007829|PDB:4NA1"
FT STRAND 3770..3778
FT /evidence="ECO:0007829|PDB:4NA1"
FT STRAND 3795..3803
FT /evidence="ECO:0007829|PDB:4NA1"
FT HELIX 3804..3819
FT /evidence="ECO:0007829|PDB:4NA1"
FT HELIX 3825..3827
FT /evidence="ECO:0007829|PDB:4NA1"
FT HELIX 3828..3837
FT /evidence="ECO:0007829|PDB:4NA1"
FT STRAND 3843..3852
FT /evidence="ECO:0007829|PDB:4NA1"
FT HELIX 3853..3865
FT /evidence="ECO:0007829|PDB:4NA1"
FT STRAND 3870..3877
FT /evidence="ECO:0007829|PDB:4NA1"
FT HELIX 3878..3880
FT /evidence="ECO:0007829|PDB:4NA1"
FT HELIX 3884..3890
FT /evidence="ECO:0007829|PDB:4NA1"
FT HELIX 3892..3903
FT /evidence="ECO:0007829|PDB:4NA1"
FT HELIX 3907..3915
FT /evidence="ECO:0007829|PDB:4NA1"
FT HELIX 3922..3925
FT /evidence="ECO:0007829|PDB:4NA1"
FT STRAND 3969..3979
FT /evidence="ECO:0007829|PDB:5KTK"
FT STRAND 3990..3996
FT /evidence="ECO:0007829|PDB:5KTK"
FT HELIX 3998..4000
FT /evidence="ECO:0007829|PDB:5KTK"
FT HELIX 4001..4008
FT /evidence="ECO:0007829|PDB:5KTK"
FT STRAND 4012..4018
FT /evidence="ECO:0007829|PDB:5KTK"
FT HELIX 4031..4033
FT /evidence="ECO:0007829|PDB:5KTK"
FT STRAND 4034..4039
FT /evidence="ECO:0007829|PDB:5KTK"
FT HELIX 4041..4043
FT /evidence="ECO:0007829|PDB:5KTK"
FT HELIX 4053..4063
FT /evidence="ECO:0007829|PDB:5KTK"
FT STRAND 4069..4077
FT /evidence="ECO:0007829|PDB:5KTK"
FT HELIX 4091..4103
FT /evidence="ECO:0007829|PDB:5KTK"
FT STRAND 4107..4114
FT /evidence="ECO:0007829|PDB:5KTK"
FT HELIX 4120..4131
FT /evidence="ECO:0007829|PDB:5KTK"
FT STRAND 4138..4143
FT /evidence="ECO:0007829|PDB:5KTK"
FT STRAND 4146..4154
FT /evidence="ECO:0007829|PDB:5KTK"
FT TURN 4156..4158
FT /evidence="ECO:0007829|PDB:5KTK"
FT STRAND 4172..4177
FT /evidence="ECO:0007829|PDB:5KTK"
FT HELIX 4182..4194
FT /evidence="ECO:0007829|PDB:5KTK"
FT STRAND 4199..4205
FT /evidence="ECO:0007829|PDB:5KTK"
FT HELIX 4211..4217
FT /evidence="ECO:0007829|PDB:5KTK"
FT HELIX 4223..4236
FT /evidence="ECO:0007829|PDB:5KTK"
FT STRAND 4240..4245
FT /evidence="ECO:0007829|PDB:5KTK"
FT HELIX 4251..4264
FT /evidence="ECO:0007829|PDB:5KTK"
FT STRAND 4268..4273
FT /evidence="ECO:0007829|PDB:5KTK"
FT HELIX 4285..4287
FT /evidence="ECO:0007829|PDB:5KTK"
FT HELIX 4290..4297
FT /evidence="ECO:0007829|PDB:5KTK"
FT TURN 4298..4301
FT /evidence="ECO:0007829|PDB:5KTK"
FT HELIX 4302..4311
FT /evidence="ECO:0007829|PDB:5KTK"
FT STRAND 4319..4324
FT /evidence="ECO:0007829|PDB:5KTK"
FT HELIX 4325..4327
FT /evidence="ECO:0007829|PDB:5KTK"
FT HELIX 4330..4333
FT /evidence="ECO:0007829|PDB:5KTK"
FT HELIX 4337..4353
FT /evidence="ECO:0007829|PDB:5KTK"
FT TURN 4354..4356
FT /evidence="ECO:0007829|PDB:5KTK"
FT STRAND 4359..4364
FT /evidence="ECO:0007829|PDB:5KTK"
FT STRAND 4367..4370
FT /evidence="ECO:0007829|PDB:5KTK"
FT HELIX 4378..4383
FT /evidence="ECO:0007829|PDB:5KTK"
FT HELIX 4390..4402
FT /evidence="ECO:0007829|PDB:5KTK"
FT STRAND 4407..4414
FT /evidence="ECO:0007829|PDB:5KTK"
FT HELIX 4421..4423
FT /evidence="ECO:0007829|PDB:5KTK"
SQ SEQUENCE 5043 AA; 562814 MW; F6E8A8533D518DE4 CRC64;
MRNNDNIRIL TNPSVSHGEP LHISEKQPAT IPEVLYRTAT ELGDTKGIIY LQPDGTEVYQ
SYRRLWDDGL RIAKGLRQSG LKAKQSVILQ LGDNSQLLPA FWGCVLTGVV PAPLAVPPTY
AESSSGTQKL KDAWTLLDKP AVITDRGMHQ EMLDWAKEQG LEGFRAIIVE DLLSAEADTD
WHQSSPEDLA LLLLTSGSTG TPKAVMLNHR NIMSMVKGII QMQGFTREDI TFNWMPFDHV
GGIGMLHLRD VYLGCQEINV SSETILMEPL KWLDWIDHYR ASVTWAPNFA FGLVTDFAEE
IKDKKWDLSS MRYMLNGGEA MVAKVGRRIL ELLEPHGLPA DAIRPAWGMS ETSSGVIFSH
EFTRAGTSDD DHFVEIGSPI PGFSMRIVND HNELVEEGEI GRFQVSGLSV TSGYYQRPDL
NESVFTEDGW FETGDLGFLR NGRLTITGRT KDAIIINGIN YYSHAIESAV EELPEIETSY
TAACAVRLGQ NSTDQLAIFF VTSAKLNDEQ MSQLLRNIQS HVSQVIGVTP EYLLPVQKEE
IPKTAIGKIQ RTQLKTSFEN GEFDHLLHKP NRMNDAVQDE GIQQADQVKR VREEIQKHLL
TCLTEELHVS HDWVEPNANI QSLGVNSIKM MKLIRSIEKN YHIKLTAREI HQYPTIERLA
SYLSEHEDLS SLSADKKGTD TYKTEPERSQ ATFQPLSEVQ KGLWTLQKMS PEKSAYHVPL
CFKFSSGLHH ETFQQAFGLV LNQHPILKHV IQEKDGVPFL KNEPALSIEI KTENISSLKE
SDIPAFLRKK VKEPYVKENS PLVRVMSFSR SEQEHFLLVV IHHLIFDGVS SVTFIRSLFD
TYQLLLKGQQ PEKAVSPAIY HDFAAWEKNM LAGKDGVKHR TYWQKQLSGT LPNLQLPNVS
ASSVDSQFRE DTYTRRLSSG FMNQVRTFAK EHSVNVTTVF LSCYMMLLGR YTGQKEQIVG
MPAMVRPEER FDDAIGHFLN MLPIRSELNP ADTFSSFISK LQLTILDGLD HAAYPFPKMV
RDLNIPRSQA GSPVFQTAFF YQNFLQSGSY QSLLSRYADF FSVDFVEYIH QEGEYELVFE
LWETEEKMEL NIKYNTGLFD AASISAMFDH FVYVTEQAML NPSQPLKEYS LLPEAEKQMI
LKTWNATGKT YPYITFHELF EQQAKKTPDR AAVSYEGQTL TYRELDEKST QLAIYLQAHG
VGPDRLAGIY VDRSLDMLVG LLAILKAGGA YVPLDPSYPA ERLEYMLEDS EVFITLTTSE
LVNTLSWNGV TTALLDQDWD EIAQTASDRK VLTRTVTPEN LAYVIYTSGS TGKPKGVMIP
HKALTNFLVS MGETPGLTAE DKMLAVTTYC FDIAALELFL PLIKGAHCYI CQTEHTKDVE
KLKRDIRAIK PTVMQATPAT WKMLFYSGWE NEESVKILCG GEALPETLKR YFLDTGSEAW
NMFGPTETTI WSAVQRINVE CSHATIGRPI ANTQIYITDS QLAPVPAGVP GELCIAGDGV
AKGYYKKEEL TDSRFIDNPF EPGSKLYRTG DMARWLTGGR IEYIGRIDNQ VKIRGFRIEL
GDIESRLSEH PGILECVVVA DMDNLAAYYT AKHANASLTA RELRHFVKNA LPAYMVPSYF
IQLDHMPLTP NGKIDRNSLK NIDLSGEQLK QRQTSPKNIQ DTVFTIWQEV LKTSDIEWDD
GFFDVGGDSL LAVTVADRIK HELSCEFSVT DLFEYSTIKN ISQYITEQRM GDASDHIPTD
PAAHIEDQST EMSDLPDYYD DSVAIIGISC EFPGAKNHDE FWENLRDGKE SIAFFNKEEL
QRFGISKEIA ENADYVPAKA SIDGKDRFDP SFFQISPKDA EFMDPQLRML LTHSWKAIED
AGYAARQIPQ TSVFMSASNN SYRALLPSDT TESLETPDGY VSWVLAQSGT IPTMISHKLG
LRGPSYFVHA NCSSSLIGLH SAYKSLLSGE SDYALVGGAT LHTESNIGYV HQPGLNFSSD
GHIKAFDASA DGMIGGEGVA VVLLKKAADA VKDGDHIYAL LRGIGVNNDG ADKVGFYAPS
VKGQADVVQQ VMNQTKVQPE SICYVEAHGT GTKLGDPIEL AALTNVYRQY TNKTQFCGIG
SVKTNIGHLD TAAGLAGCIK VVMSLYHQEL APSVNYKEPN PNTDLASSPF YVVDQKKTLS
REIKTHRAAL SSFGLGGTNT HAIFEQFKRD SDKGKIDGTC IVPISAKNKE RLQEYAEDIL
AYLERRGFEN SQLPDFAYTL QVGREAMEHR VVFIADHVNE LKQRLTDFIN GNTAIEGCFQ
GSKHNAREVS WLTEDEDSAE LIRKWMAKGK VNKLAEMWSK GAHIDWMQLY KGERPNRMSL
PTYPFAKERY WPSQDDRKPV AQISGNQTGI GSIHPLLHQN TSDFSEQKFS SVFTGDEFFL
RDHVVRGKPV LPGVAYLEMA YAAINQAAGS EIGQDVRIRL NHTVWVQPVV VDRHSAQVDI
SLFPEEDGKI TFDIYSTQED GDDPVIHSQG SAELASAAET PVADLTEMSR RCGKGKMSPD
QFYEEGRSRG MFHGPAFQGI KNVNIGNREV LAQLQLPEIV SGTNEQFVLH PSIMDSALQT
ATICIMQELT DQKLILPFAL EELEVIKGCS SSMWAYARLS DSDHSGGVVQ KADIDVIDES
GTVCVRIKGF STRVLEGEVH TSKPSTRHER LMLEPVWEKQ NEEREDEDLS YTEHIIVLFE
TERSVTDSIA SHMKDARVIT LNEAVGHIAE RYQCYMQNIF ELLQSKVRKL SAGRIIIQAI
VPLEKEKQLF AGVSGLFKTA EIEFSKLTAQ VIEIEKPEEM IDLHLKLKDD SRRPFDKQIR
YEAGYRFVKG WREMVLPSAD TLHMPWRDEG VYLITGGAGS LGLLFAKEIA NRTGRSTIVL
TGRSVLSEDK ENELEALRSI GAEVVYREAD VSDQHAVRHL LEEIKERYGT LNGIIHGAGS
SKDRFIIHKT NEEFQEVLQP KVSGLLHVDE CSKDFPLDFF IFFSSVSGCL GNAGQADYAA
ANSFMDAFAE YRRSLAASKK RFGSTISFNW PLWEEGGMQV GAEDEKRMLK TTGMVPMPTD
SGLKAFYQGI VSDKPQVFVM EGQLQKMKQK LLSAGSKAKR NDQRKADQDQ GQTRKLEAAL
IQMVGAILKV NTDDIDVNTE LSEYGFDSVT FTVFTNKINE KFQLELTPTI FFEYGSVQSL
AEYVVAAYQG EWNQDATAKG KDERTNLVHS LSSLEASLSN MVSAILKVNS EDIDVNTELS
EYGFDSVTFT VFTNKINEEF QLELTPTIFF EYGSLHSLAE YLTVEHGDTL VQEREKPEGQ
EELQTKSSEA PKITSRRKRR FTQPIIAKAE RNKKQAADFE PVAIVGISGR FPGAMDIDEF
WKNLEEGKDS ITEVPKDRWD WREHYGNPDT DVNKTDIKWG GFIDGVAEFD PLFFGISPRE
ADYVDPQQRL LMTYVWKALE DAGCSPQSLS GTGTGIFIGT GNTGYKDLFH RANLPIEGHA
ATGHMIPSVG PNRMSYFLNI HGPSEPVETA CSSSLVAIHR AVTAMQNGDC EMAIAGGVNT
ILTEEAHISY SKAGMLSTDG RCKTFSADAN GYVRGEGVGM VMLKKLEDAE RDGNHIYGVI
RGTAENHGGR ANTLTSPNPK AQADLLVRAY RQADIDPSTV TYIEAHGTGT ELGDPIEING
LKAAFKELSN MRGESQPDVP DHRCGIGSVK SNIGHLELAA GISGLIKVLL QMKHKTLVKS
LHCETLNPYL QLTDSPFYIV QEKQEWKSVT DRDGNELPRR AGISSFGIGG VNAHIVIEEY
MPKANSEHTA TEQPNVIVLS AKNKSRLIDR ASQLLEVIRN KKYTDQDLHR IAYTLQVGRE
EMDERLACVA GTMQELEEKL QAFVDGKEET DEFFRGQSHR NKETQTIFTA DEDMALALDA
WIRKRKYAKL ADLWVKGVSI QWNTLYGETK PRLISLPSYP FAKDHYWVPA KEHSERDKKE
LVNAIEDRAA CFLTKQWSLS PIGSAVPGTR TVAILCCQET ADLAAEVSSY FPNHLLIDVS
RIENDQSDID WKEFDGLVDV IGCGWDDEGR LDWIEWVQRL VEFGHKEGLR LLCVTKGLES
FQNTSVRMAG ASRAGLYRML QCEYSHLISR HMDAEEVTDH RRLAKLIADE FYSDSYDAEV
CYRDGLRYQA FLKAHPETGK ATEQSAVFPK DHVLLITGGT RGIGLLCARH FAECYGVKKL
VLTGREQLPP REEWARFKTS NTSLAEKIQA VRELEAKGVQ VEMLSLTLSD DAQVEQTLQH
IKRTLGPIGG VIHCAGLTDM DTLAFIRKTS DDIQRVLEPK VSGLTTLYRH VCNEPLQFFV
LFSSVSAIIP ELSAGQADYA MANSYMDYFA EAHQKHAPII SVQWPNWKET GMGEVTNQAY
RDSGLLSITN SEGLRFLDQI VSKKFGPVVL PAMANQTNWE PELLMKRRKP HEGGLQEAAL
QSPPARDIEE ADEVSKCDGL LSETQSWLID LFTEELRIDR EDFEIDGLFQ DYGVDSIILA
QVLQRINRKL EAALDPSILY EYPTIQRFAD WLIGSYSERL SALFGGRISD ASAPLENKIE
AEASVPGKDR ALTPQIQAPA ILSPDSHAEG IAVVGLSCRF PGAETLESYW SLLSEGRSSI
GPIPAERWGC KTPYYAGVID GVSYFDPDFF LLHEEDVRAM DPQALLVLEE CLKLLYHAGY
TPEEIKGKPV GVYIGGRSQH KPDEDSLDHA KNPIVTVGQN YLAANLSQFF DVRGPSVVVD
TACSSALVGM NMAIQALRGG DIQSAIVGGV SLLSSDASHR LFDRRGILSK HSSFHVFDER
ADGVVLGEGV GMVMLKTVKQ ALEDGDIIYA VVKAASVNND GRTAGPATPN LEAQKEVMKD
ALFKSGKKPE DISYLEANGS GSIVTDLLEL KAIQSVYRSG HSSPLSLGSI KPNIGHPLCA
EGIASFIKVV LMLKERRFVP FLSGEKEMAH FDQQKANITF SRALEKWTDS QPTAAINCFA
DGGTNAHVIV EAWEKDEKHA IKRSPISPPQ LKKRMLSPGE PKLEAETSKM TAANIWDTYE
VEV
