FTSX_BACSU
ID FTSX_BACSU Reviewed; 296 AA.
AC O34876;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Cell division protein FtsX;
GN Name=ftsX; OrderedLocusNames=BSU35250;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Lazarevic V., Soldo B., Rivolta C., Reynolds S., Mauel C., Karamata D.;
RT "Nucleotide sequence of the 300-304 chromosomal segment of Bacillus
RT subtilis.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
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 FUNCTION IN SPORULATION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / PY79;
RX PubMed=18573177; DOI=10.1111/j.1365-2958.2008.06340.x;
RA Garti-Levi S., Hazan R., Kain J., Fujita M., Ben-Yehuda S.;
RT "The FtsEX ABC transporter directs cellular differentiation in Bacillus
RT subtilis.";
RL Mol. Microbiol. 69:1018-1028(2008).
RN [4]
RP INTERACTION WITH FLOT, AND SUBCELLULAR LOCATION.
RC STRAIN=168;
RX PubMed=23651456; DOI=10.1111/mmi.12252;
RA Bach J.N., Bramkamp M.;
RT "Flotillins functionally organize the bacterial membrane.";
RL Mol. Microbiol. 88:1205-1217(2013).
CC -!- FUNCTION: Part of the ABC transporter FtsEX involved in asymmetric
CC cellular division facilitating the initiation of sporulation. May act
CC as an importer, possibly at the top of a hierarchical cascade leading
CC to the correct temporal initiation of sporulation. Acts upstream of the
CC histidine kinases KinA, KinB and KinC, the RapA phosphatase and the
CC Spo0A sporulation protein. {ECO:0000269|PubMed:18573177}.
CC -!- SUBUNIT: Interacts with FtsE (Probable). Interacts with FloT
CC (PubMed:23651456). {ECO:0000269|PubMed:23651456, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23651456,
CC ECO:0000305|PubMed:18573177}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:18573177}. Membrane raft
CC {ECO:0000269|PubMed:23651456}; Multi-pass membrane protein. Note=Unlike
CC the E.coli ortholog, localization is not restricted to division septa,
CC nor is it dependent on FtsZ. Present in detergent-resistant membrane
CC (DRM) fractions that may be equivalent to eukaryotic membrane rafts;
CC these rafts include proteins involved in signaling, molecule
CC trafficking and protein secretion (PubMed:23651456).
CC {ECO:0000269|PubMed:23651456}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene and ftsE, the previous
CC gene in the operon, delay sporulation onset, as a result of which they
CC form a medial rather than polar septum at the onset of sporulation.
CC This is presumably due to slower phosphorylation and activation of the
CC spo0A transcriptional regulator. However, at later time points these
CC cells undergo polar division and eventually form smaller than wild-type
CC mature spores. {ECO:0000269|PubMed:18573177}.
CC -!- SIMILARITY: Belongs to the ABC-4 integral membrane protein family. FtsX
CC subfamily. {ECO:0000305}.
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DR EMBL; AF017113; AAC67264.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15542.1; -; Genomic_DNA.
DR PIR; G69627; G69627.
DR RefSeq; NP_391405.1; NC_000964.3.
DR RefSeq; WP_009968247.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; O34876; -.
DR SMR; O34876; -.
DR STRING; 224308.BSU35250; -.
DR jPOST; O34876; -.
DR PaxDb; O34876; -.
DR PRIDE; O34876; -.
DR EnsemblBacteria; CAB15542; CAB15542; BSU_35250.
DR GeneID; 936708; -.
DR KEGG; bsu:BSU35250; -.
DR PATRIC; fig|224308.179.peg.3815; -.
DR eggNOG; COG2177; Bacteria.
DR InParanoid; O34876; -.
DR OMA; ETGIMRL; -.
DR PhylomeDB; O34876; -.
DR BioCyc; BSUB:BSU35250-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0008356; P:asymmetric cell division; IGI:UniProtKB.
DR GO; GO:0090529; P:cell septum assembly; IGI:UniProtKB.
DR GO; GO:0045881; P:positive regulation of sporulation resulting in formation of a cellular spore; IGI:UniProtKB.
DR GO; GO:0070297; P:regulation of phosphorelay signal transduction system; IMP:UniProtKB.
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 Cell cycle; Cell division; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..296
FT /note="Cell division protein FtsX"
FT /id="PRO_0000166791"
FT TOPO_DOM 1..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..170
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..218
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..264
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 286..296
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 296 AA; 33099 MW; 194D52C7A4A43B3A CRC64;
MIKILGRHLR ESFKSLGRNT WMTFASISAV TVTLILVGVF LVIMLNLNNM ATNAEKQVEI
KVLIDLTADQ KAQDKLQNDI KELKGIQSVT FSSKEKELDQ LVDSFGDSGK SLTMKDQENP
LNDAFVVKTT DPHDTPNVAK KIEKMDHVYK VTYGKEEVSR LFKVVGVSRN IGIALIIGLV
FTAMFLISNT IKITIFARRK EIEIMKLVGA TNWFIRWPFF LEGLLLGVFG SVIPIALVLS
TYQYVIGWVV PKVQGSFVSL LPYNPFVFQV SLVLIAIGAV IGVWGSLTSI RKFLRV
