FTSX_STRP2
ID FTSX_STRP2 Reviewed; 308 AA.
AC Q04LE4;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Cell division protein FtsX {ECO:0000250|UniProtKB:O34876, ECO:0000312|EMBL:ABJ54921.1};
GN Name=ftsX {ECO:0000312|EMBL:ABJ54921.1}; OrderedLocusNames=SPD_0660;
OS Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=373153;
RN [1] {ECO:0000312|EMBL:ABJ54921.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D39 / NCTC 7466;
RX PubMed=17041037; DOI=10.1128/jb.01148-06;
RA Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M.,
RA Wayne K.J., Tettelin H., Glass J.I., Winkler M.E.;
RT "Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus
RT pneumoniae and comparison with that of unencapsulated laboratory strain
RT R6.";
RL J. Bacteriol. 189:38-51(2007).
RN [2] {ECO:0000305}
RP INTERACTION WITH FTSE AND PCSB, SUBCELLULAR LOCATION, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=22006325; DOI=10.1073/pnas.1108323108;
RA Sham L.T., Barendt S.M., Kopecky K.E., Winkler M.E.;
RT "Essential PcsB putative peptidoglycan hydrolase interacts with the
RT essential FtsXSpn cell division protein in Streptococcus pneumoniae D39.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:E1061-E1069(2011).
CC -!- FUNCTION: Part of the ABC transporter FtsEX involved in asymmetric
CC cellular division facilitating the initiation of sporulation.
CC {ECO:0000250|UniProtKB:O34876}.
CC -!- SUBUNIT: Interacts with FtsE. Interacts (via large extracellular loop)
CC with PcsB (via N-terminal coiled coil domain). This interaction directs
CC PcsB to equatorial and septal sites of dividing cells.
CC {ECO:0000269|PubMed:22006325}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22006325};
CC Multi-pass membrane protein {ECO:0000255, ECO:0000269|PubMed:22006325}.
CC -!- SIMILARITY: Belongs to the ABC-4 integral membrane protein family. FtsX
CC subfamily. {ECO:0000255}.
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DR EMBL; CP000410; ABJ54921.1; -; Genomic_DNA.
DR RefSeq; WP_000625533.1; NC_008533.2.
DR PDB; 6HE6; X-ray; 2.00 A; A/B=49-165.
DR PDB; 6HEE; X-ray; 2.30 A; A/B=49-165.
DR PDB; 6HFX; X-ray; 2.16 A; A/B=52-165.
DR PDB; 6MK7; NMR; -; A=47-168.
DR PDBsum; 6HE6; -.
DR PDBsum; 6HEE; -.
DR PDBsum; 6HFX; -.
DR PDBsum; 6MK7; -.
DR AlphaFoldDB; Q04LE4; -.
DR BMRB; Q04LE4; -.
DR SMR; Q04LE4; -.
DR STRING; 373153.SPD_0660; -.
DR EnsemblBacteria; ABJ54921; ABJ54921; SPD_0660.
DR KEGG; spd:SPD_0660; -.
DR eggNOG; COG2177; Bacteria.
DR HOGENOM; CLU_073546_2_2_9; -.
DR OMA; ETGIMRL; -.
DR OrthoDB; 1653234at2; -.
DR BioCyc; SPNE373153:G1G6V-726-MON; -.
DR Proteomes; UP000001452; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR InterPro; IPR003838; ABC3_permease_dom.
DR InterPro; IPR004513; ABC_transpt_FtsX.
DR InterPro; IPR040690; FtsX_ECD.
DR PANTHER; PTHR47755; PTHR47755; 1.
DR Pfam; PF02687; FtsX; 1.
DR Pfam; PF18075; FtsX_ECD; 1.
DR PIRSF; PIRSF003097; FtsX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cell membrane; Membrane;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..308
FT /note="Cell division protein FtsX"
FT /id="PRO_0000421664"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..178
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 200..236
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 258..276
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 298..308
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:6HE6"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:6HE6"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:6HE6"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:6HE6"
FT TURN 85..88
FT /evidence="ECO:0007829|PDB:6HE6"
FT HELIX 89..95
FT /evidence="ECO:0007829|PDB:6HE6"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:6HE6"
FT HELIX 108..118
FT /evidence="ECO:0007829|PDB:6HE6"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:6HE6"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:6HE6"
FT STRAND 136..143
FT /evidence="ECO:0007829|PDB:6HE6"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:6HE6"
FT HELIX 147..155
FT /evidence="ECO:0007829|PDB:6HE6"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:6HE6"
SQ SEQUENCE 308 AA; 34270 MW; CBC96434D1F5716B CRC64;
MISRFFRHLF EALKSLKRNG WMTVAAVSSV MITLTLVAIF ASVIFNTAKL ATDIENNVRV
VVYIRKDVED NSQTIEKEGQ TVTNNDYHKV YDSLKNMSTV KSVTFSSKEE QYEKLTEIMG
DNWKIFEGDA NPLYDAYIVE ANAPNDVKTI AEDAKKIEGV SEVQDGGANT ERLFKLASFI
RVWGLGIAAL LIFIAVFLIS NTIRITIISR SREIQIMRLV GAKNSYIRGP FLLEGAFIGL
LGAIAPSVLV FIVYQIVYQS VNKSLVGQNL SMISPDLFSP LMIALLFVIG VFIGSLGSGI
SMRRFLKI
