GenomeNet

Database: UniProt
Entry: Q9F1K9
LinkDB: Q9F1K9
Original site: Q9F1K9 
ID   PSBK_THEEB              Reviewed;          46 AA.
AC   Q9F1K9;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   02-DEC-2020, entry version 119.
DE   RecName: Full=Photosystem II reaction center protein K {ECO:0000255|HAMAP-Rule:MF_00441};
DE            Short=PSII-K {ECO:0000255|HAMAP-Rule:MF_00441};
DE   Flags: Precursor;
GN   Name=psbK {ECO:0000255|HAMAP-Rule:MF_00441}; OrderedLocusNames=tsl0176;
OS   Thermosynechococcus elongatus (strain BP-1).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Thermosynechococcus.
OX   NCBI_TaxID=197221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Katoh H., Ikeuchi M.;
RT   "Cloning and disruption of the psbK gene from thermophilic
RT   Thermosynechococcus elongatus.";
RL   Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BP-1;
RX   PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA   Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA   Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA   Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takeuchi C., Yamada M., Tabata S.;
RT   "Complete genome structure of the thermophilic cyanobacterium
RT   Thermosynechococcus elongatus BP-1.";
RL   DNA Res. 9:123-130(2002).
RN   [3]
RP   PROTEIN SEQUENCE OF 10-24, PROPEPTIDE, COFACTOR, AND SUBCELLULAR LOCATION.
RX   PubMed=17935689; DOI=10.1016/j.bbabio.2007.08.008;
RA   Kashino Y., Takahashi T., Inoue-Kashino N., Ban A., Ikeda Y., Satoh K.,
RA   Sugiura M.;
RT   "Ycf12 is a core subunit in the photosystem II complex.";
RL   Biochim. Biophys. Acta 1767:1269-1275(2007).
RN   [4]
RP   PROTEIN SEQUENCE OF 10-19, COFACTOR, AND SUBCELLULAR LOCATION.
RX   PubMed=17967798; DOI=10.1093/pcp/pcm148;
RA   Iwai M., Suzuki T., Dohmae N., Inoue Y., Ikeuchi M.;
RT   "Absence of the PsbZ subunit prevents association of PsbK and Ycf12 with
RT   the PSII complex in the thermophilic cyanobacterium Thermosynechococcus
RT   elongatus BP-1.";
RL   Plant Cell Physiol. 48:1758-1763(2007).
RN   [5]
RP   PROTEIN SEQUENCE OF 10-16, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=BP-1;
RX   PubMed=20194360; DOI=10.1093/pcp/pcq020;
RA   Iwai M., Suzuki T., Kamiyama A., Sakurai I., Dohmae N., Inoue Y.,
RA   Ikeuchi M.;
RT   "The PsbK subunit is required for the stable assembly and stability of
RT   other small subunits in the PSII complex in the thermophilic cyanobacterium
RT   Thermosynechococcus elongatus BP-1.";
RL   Plant Cell Physiol. 51:554-560(2010).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 10-46 IN PHOTOSYSTEM II,
RP   COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=14764885; DOI=10.1126/science.1093087;
RA   Ferreira K.N., Iverson T.M., Maghlaoui K., Barber J., Iwata S.;
RT   "Architecture of the photosynthetic oxygen-evolving center.";
RL   Science 303:1831-1838(2004).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 10-46 IN PHOTOSYSTEM II,
RP   COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=BP-1;
RX   PubMed=16355230; DOI=10.1038/nature04224;
RA   Loll B., Kern J., Saenger W., Zouni A., Biesiadka J.;
RT   "Towards complete cofactor arrangement in the 3.0 A resolution structure of
RT   photosystem II.";
RL   Nature 438:1040-1044(2005).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 10-46 IN PHOTOSYSTEM II,
RP   COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND TOPOLOGY.
RC   STRAIN=BP-1;
RX   PubMed=19219048; DOI=10.1038/nsmb.1559;
RA   Guskov A., Kern J., Gabdulkhakov A., Broser M., Zouni A., Saenger W.;
RT   "Cyanobacterial photosystem II at 2.9-A resolution and the role of
RT   quinones, lipids, channels and chloride.";
RL   Nat. Struct. Mol. Biol. 16:334-342(2009).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) OF 10-46 IN PHOTOSYSTEM II,
RP   FUNCTION, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC   STRAIN=BP-1;
RX   PubMed=20558739; DOI=10.1074/jbc.m110.127589;
RA   Broser M., Gabdulkhakov A., Kern J., Guskov A., Muh F., Saenger W.,
RA   Zouni A.;
RT   "Crystal structure of monomeric photosystem II from Thermosynechococcus
RT   elongatus at 3.6 A resolution.";
RL   J. Biol. Chem. 285:26255-26262(2010).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 10-46 IN PHOTOSYSTEM II,
RP   FUNCTION, COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=21367867; DOI=10.1074/jbc.m110.215970;
RA   Broser M., Glockner C., Gabdulkhakov A., Guskov A., Buchta J., Kern J.,
RA   Muh F., Dau H., Saenger W., Zouni A.;
RT   "Structural basis of cyanobacterial photosystem II inhibition by the
RT   herbicide terbutryn.";
RL   J. Biol. Chem. 286:15964-15972(2011).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (6.56 ANGSTROMS) OF 10-46 IN PHOTOSYSTEM II,
RP   COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=BP-1;
RX   PubMed=22665786; DOI=10.1073/pnas.1204598109;
RA   Kern J., Alonso-Mori R., Hellmich J., Tran R., Hattne J., Laksmono H.,
RA   Glockner C., Echols N., Sierra R.G., Sellberg J., Lassalle-Kaiser B.,
RA   Gildea R.J., Glatzel P., Grosse-Kunstleve R.W., Latimer M.J., McQueen T.A.,
RA   DiFiore D., Fry A.R., Messerschmidt M., Miahnahri A., Schafer D.W.,
RA   Seibert M.M., Sokaras D., Weng T.C., Zwart P.H., White W.E., Adams P.D.,
RA   Bogan M.J., Boutet S., Williams G.J., Messinger J., Sauter N.K., Zouni A.,
RA   Bergmann U., Yano J., Yachandra V.K.;
RT   "Room temperature femtosecond X-ray diffraction of photosystem II
RT   microcrystals.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:9721-9726(2012).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (5.70 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=BP-1;
RX   PubMed=23413188; DOI=10.1126/science.1234273;
RA   Kern J., Alonso-Mori R., Tran R., Hattne J., Gildea R.J., Echols N.,
RA   Glockner C., Hellmich J., Laksmono H., Sierra R.G., Lassalle-Kaiser B.,
RA   Koroidov S., Lampe A., Han G., Gul S., Difiore D., Milathianaki D.,
RA   Fry A.R., Miahnahri A., Schafer D.W., Messerschmidt M., Seibert M.M.,
RA   Koglin J.E., Sokaras D., Weng T.C., Sellberg J., Latimer M.J.,
RA   Grosse-Kunstleve R.W., Zwart P.H., White W.E., Glatzel P., Adams P.D.,
RA   Bogan M.J., Williams G.J., Boutet S., Messinger J., Zouni A., Sauter N.K.,
RA   Yachandra V.K., Bergmann U., Yano J.;
RT   "Simultaneous femtosecond X-ray spectroscopy and diffraction of photosystem
RT   II at room temperature.";
RL   Science 340:491-495(2013).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (5.00 ANGSTROMS) OF 10-46 IN PHOTOSYSTEM II,
RP   COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=BP-1;
RX   PubMed=25043005; DOI=10.1038/nature13453;
RA   Kupitz C., Basu S., Grotjohann I., Fromme R., Zatsepin N.A., Rendek K.N.,
RA   Hunter M.S., Shoeman R.L., White T.A., Wang D., James D., Yang J.H.,
RA   Cobb D.E., Reeder B., Sierra R.G., Liu H., Barty A., Aquila A.L.,
RA   Deponte D., Kirian R.A., Bari S., Bergkamp J.J., Beyerlein K.R.,
RA   Bogan M.J., Caleman C., Chao T.C., Conrad C.E., Davis K.M.,
RA   Fleckenstein H., Galli L., Hau-Riege S.P., Kassemeyer S., Laksmono H.,
RA   Liang M., Lomb L., Marchesini S., Martin A.V., Messerschmidt M.,
RA   Milathianaki D., Nass K., Ros A., Roy-Chowdhury S., Schmidt K., Seibert M.,
RA   Steinbrener J., Stellato F., Yan L., Yoon C., Moore T.A., Moore A.L.,
RA   Pushkar Y., Williams G.J., Boutet S., Doak R.B., Weierstall U., Frank M.,
RA   Chapman H.N., Spence J.C., Fromme P.;
RT   "Serial time-resolved crystallography of photosystem II using a femtosecond
RT   X-ray laser.";
RL   Nature 513:261-265(2014).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (4.50 ANGSTROMS) IN PHOTOSYSTEM II, FUNCTION,
RP   COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=BP-1;
RX   PubMed=25006873; DOI=10.1038/ncomms5371;
RA   Kern J., Tran R., Alonso-Mori R., Koroidov S., Echols N., Hattne J.,
RA   Ibrahim M., Gul S., Laksmono H., Sierra R.G., Gildea R.J., Han G.,
RA   Hellmich J., Lassalle-Kaiser B., Chatterjee R., Brewster A.S., Stan C.A.,
RA   Gloeckner C., Lampe A., DiFiore D., Milathianaki D., Fry A.R.,
RA   Seibert M.M., Koglin J.E., Gallo E., Uhlig J., Sokaras D., Weng T.C.,
RA   Zwart P.H., Skinner D.E., Bogan M.J., Messerschmidt M., Glatzel P.,
RA   Williams G.J., Boutet S., Adams P.D., Zouni A., Messinger J., Sauter N.K.,
RA   Bergmann U., Yano J., Yachandra V.K.;
RT   "Taking snapshots of photosynthetic water oxidation using femtosecond X-ray
RT   diffraction and spectroscopy.";
RL   Nat. Commun. 5:4371-4371(2014).
CC   -!- FUNCTION: One of the components of the core complex of photosystem II
CC       (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that
CC       uses light energy to abstract electrons from H(2)O, generating O(2) and
CC       a proton gradient subsequently used for ATP formation. It consists of a
CC       core antenna complex that captures photons, and an electron transfer
CC       chain that converts photonic excitation into a charge separation.
CC       Required for association of PsbZ and Ycf12 with PSII (PubMed:20194360).
CC       {ECO:0000255|HAMAP-Rule:MF_00441, ECO:0000269|PubMed:20194360,
CC       ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:21367867,
CC       ECO:0000269|PubMed:25006873}.
CC   -!- COFACTOR:
CC       Note=PSII binds multiple chlorophylls, carotenoids and specific lipids.
CC       {ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230,
CC       ECO:0000269|PubMed:17935689, ECO:0000269|PubMed:17967798,
CC       ECO:0000269|PubMed:19219048, ECO:0000269|PubMed:20558739,
CC       ECO:0000269|PubMed:21367867, ECO:0000269|PubMed:22665786,
CC       ECO:0000269|PubMed:23413188, ECO:0000269|PubMed:25006873,
CC       ECO:0000269|PubMed:25043005};
CC   -!- SUBUNIT: Cyanobacterial PSII is composed of 1 copy each of membrane
CC       proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK,
CC       PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral
CC       proteins PsbO, PsbU, PsbV and a large number of cofactors. It forms
CC       dimeric complexes. {ECO:0000255|HAMAP-Rule:MF_00441,
CC       ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230,
CC       ECO:0000269|PubMed:19219048, ECO:0000269|PubMed:20194360,
CC       ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:21367867,
CC       ECO:0000269|PubMed:22665786, ECO:0000269|PubMed:23413188,
CC       ECO:0000269|PubMed:25006873, ECO:0000269|PubMed:25043005}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00441, ECO:0000269|PubMed:14764885,
CC       ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:17935689,
CC       ECO:0000269|PubMed:17967798, ECO:0000269|PubMed:19219048,
CC       ECO:0000269|PubMed:20194360, ECO:0000269|PubMed:20558739,
CC       ECO:0000269|PubMed:21367867, ECO:0000269|PubMed:22665786,
CC       ECO:0000269|PubMed:23413188, ECO:0000269|PubMed:25006873,
CC       ECO:0000269|PubMed:25043005}; Single-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_00441, ECO:0000269|PubMed:14764885,
CC       ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:17935689,
CC       ECO:0000269|PubMed:17967798, ECO:0000269|PubMed:19219048,
CC       ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:21367867,
CC       ECO:0000269|PubMed:22665786, ECO:0000269|PubMed:23413188,
CC       ECO:0000269|PubMed:25006873, ECO:0000269|PubMed:25043005}.
CC   -!- MASS SPECTROMETRY: Mass=4103; Mass_error=4; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:19219048};
CC   -!- MASS SPECTROMETRY: Mass=4101; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:20558739};
CC   -!- DISRUPTION PHENOTYPE: No changes in growth under low, medium or high
CC       light regimes (3-300 umol photon7/(2)/s). PsbZ and Ycf12 are missing
CC       from isolated PSII, although low levels of PsbZ can be detected in
CC       thylakoid membranes. {ECO:0000269|PubMed:20194360}.
CC   -!- SIMILARITY: Belongs to the PsbK family. {ECO:0000255|HAMAP-
CC       Rule:MF_00441}.
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; AB052850; BAB20628.1; -; Genomic_DNA.
DR   EMBL; BA000039; BAC07729.1; -; Genomic_DNA.
DR   RefSeq; NP_680967.1; NC_004113.1.
DR   PDB; 1S5L; X-ray; 3.50 A; K/k=10-46.
DR   PDB; 2AXT; X-ray; 3.00 A; K/k=10-46.
DR   PDB; 3KZI; X-ray; 3.60 A; K=10-46.
DR   PDB; 4FBY; X-ray; 6.56 A; K/c=10-46.
DR   PDB; 4IXQ; X-ray; 5.70 A; K/k=1-46.
DR   PDB; 4IXR; X-ray; 5.90 A; K/k=1-46.
DR   PDB; 4PBU; X-ray; 5.00 A; K/k=10-46.
DR   PDB; 4PJ0; X-ray; 2.44 A; K/k=1-46.
DR   PDB; 4RVY; X-ray; 5.50 A; K/k=10-46.
DR   PDB; 4TNH; X-ray; 4.90 A; K/k=1-46.
DR   PDB; 4TNI; X-ray; 4.60 A; K/k=1-46.
DR   PDB; 4TNJ; X-ray; 4.50 A; K/k=1-46.
DR   PDB; 4TNK; X-ray; 5.20 A; K/k=1-46.
DR   PDB; 4V62; X-ray; 2.90 A; AK/BK=10-46.
DR   PDB; 4V82; X-ray; 3.20 A; AK/BK=10-46.
DR   PDB; 5E79; X-ray; 3.50 A; K/k=10-46.
DR   PDB; 5E7C; X-ray; 4.50 A; K/k=10-46.
DR   PDB; 5H2F; X-ray; 2.20 A; K/k=10-46.
DR   PDB; 5KAF; X-ray; 3.00 A; K/k=1-46.
DR   PDB; 5KAI; X-ray; 2.80 A; K/k=1-46.
DR   PDB; 5MX2; X-ray; 2.20 A; K/k=1-46.
DR   PDB; 5TIS; X-ray; 2.25 A; K/k=1-46.
DR   PDB; 5ZZN; X-ray; 2.10 A; K/k=10-46.
DR   PDB; 6DHE; X-ray; 2.05 A; K/k=10-46.
DR   PDB; 6DHF; X-ray; 2.08 A; K/k=10-46.
DR   PDB; 6DHG; X-ray; 2.50 A; K/k=10-46.
DR   PDB; 6DHH; X-ray; 2.20 A; K/k=10-46.
DR   PDB; 6DHO; X-ray; 2.07 A; K/k=10-46.
DR   PDB; 6DHP; X-ray; 2.04 A; K/k=10-46.
DR   PDB; 6W1O; X-ray; 2.08 A; K/k=1-46.
DR   PDB; 6W1P; X-ray; 2.26 A; K/k=1-46.
DR   PDB; 6W1Q; X-ray; 2.27 A; K/k=1-46.
DR   PDB; 6W1R; X-ray; 2.23 A; K/k=1-46.
DR   PDB; 6W1T; X-ray; 2.01 A; K/k=1-46.
DR   PDB; 6W1U; X-ray; 2.09 A; K/k=1-46.
DR   PDB; 6W1V; X-ray; 2.09 A; K/k=1-46.
DR   PDBsum; 1S5L; -.
DR   PDBsum; 2AXT; -.
DR   PDBsum; 3KZI; -.
DR   PDBsum; 4FBY; -.
DR   PDBsum; 4IXQ; -.
DR   PDBsum; 4IXR; -.
DR   PDBsum; 4PBU; -.
DR   PDBsum; 4PJ0; -.
DR   PDBsum; 4RVY; -.
DR   PDBsum; 4TNH; -.
DR   PDBsum; 4TNI; -.
DR   PDBsum; 4TNJ; -.
DR   PDBsum; 4TNK; -.
DR   PDBsum; 4V62; -.
DR   PDBsum; 4V82; -.
DR   PDBsum; 5E79; -.
DR   PDBsum; 5E7C; -.
DR   PDBsum; 5H2F; -.
DR   PDBsum; 5KAF; -.
DR   PDBsum; 5KAI; -.
DR   PDBsum; 5MX2; -.
DR   PDBsum; 5TIS; -.
DR   PDBsum; 5ZZN; -.
DR   PDBsum; 6DHE; -.
DR   PDBsum; 6DHF; -.
DR   PDBsum; 6DHG; -.
DR   PDBsum; 6DHH; -.
DR   PDBsum; 6DHO; -.
DR   PDBsum; 6DHP; -.
DR   PDBsum; 6W1O; -.
DR   PDBsum; 6W1P; -.
DR   PDBsum; 6W1Q; -.
DR   PDBsum; 6W1R; -.
DR   PDBsum; 6W1T; -.
DR   PDBsum; 6W1U; -.
DR   PDBsum; 6W1V; -.
DR   SMR; Q9F1K9; -.
DR   DIP; DIP-48496N; -.
DR   IntAct; Q9F1K9; 1.
DR   STRING; 197221.22293897; -.
DR   EnsemblBacteria; BAC07729; BAC07729; BAC07729.
DR   KEGG; tel:tsl0176; -.
DR   PATRIC; fig|197221.4.peg.182; -.
DR   eggNOG; ENOG5032YQR; Bacteria.
DR   EvolutionaryTrace; Q9F1K9; -.
DR   Proteomes; UP000000440; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009539; C:photosystem II reaction center; IEA:InterPro.
DR   GO; GO:0042651; C:thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00441; PSII_PsbK; 1.
DR   InterPro; IPR003687; PSII_PsbK.
DR   InterPro; IPR037270; PSII_PsbK_sf.
DR   PANTHER; PTHR35325; PTHR35325; 1.
DR   Pfam; PF02533; PsbK; 1.
DR   SUPFAM; SSF161037; SSF161037; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Membrane; Photosynthesis;
KW   Photosystem II; Reaction center; Reference proteome; Thylakoid;
KW   Transmembrane; Transmembrane helix.
FT   PROPEP          1..9
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00441,
FT                   ECO:0000269|PubMed:17935689, ECO:0000269|PubMed:17967798"
FT                   /id="PRO_0000029543"
FT   CHAIN           10..46
FT                   /note="Photosystem II reaction center protein K"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00441"
FT                   /id="PRO_0000029544"
FT   TOPO_DOM        10..24
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   TRANSMEM        25..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   TOPO_DOM        39..46
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   HELIX           13..18
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           19..22
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           25..27
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           28..42
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   TURN            43..45
FT                   /evidence="ECO:0000244|PDB:5ZZN"
SQ   SEQUENCE   46 AA;  5026 MW;  45C5197F4B50E398 CRC64;
     MIDALVLVAK LPEAYAIFDP LVDVLPVIPV LFLALAFVWQ AAVGFR
//
DBGET integrated database retrieval system