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Database: UniProt
Entry: I3VVM4_THESW
LinkDB: I3VVM4_THESW
Original site: I3VVM4_THESW 
ID   I3VVM4_THESW            Unreviewed;       143 AA.
AC   I3VVM4;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Cell division protein FtsL {ECO:0000256|HAMAP-Rule:MF_00910};
GN   Name=ftsL {ECO:0000256|HAMAP-Rule:MF_00910};
GN   OrderedLocusNames=Tsac_1562 {ECO:0000313|EMBL:AFK86569.1};
OS   Thermoanaerobacterium saccharolyticum (strain DSM 8691 / JW/SL-YS485).
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacterium.
OX   NCBI_TaxID=1094508 {ECO:0000313|EMBL:AFK86569.1, ECO:0000313|Proteomes:UP000006178};
RN   [1] {ECO:0000313|Proteomes:UP000006178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8691 / JW/SL-YS485 {ECO:0000313|Proteomes:UP000006178};
RA   Brown S.D., Land M.L., Herring C.D.;
RT   "Thermoanaerobacterium saccharolyticum JW/SL-YS485.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AFK86569.1, ECO:0000313|Proteomes:UP000006178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8691 / JW/SL-YS485 {ECO:0000313|Proteomes:UP000006178};
RX   PubMed=24907337; DOI=10.1128/AEM.00998-14;
RA   Currie D.H., Guss A.M., Herring C.D., Giannone R.J., Johnson C.M.,
RA   Lankford P.K., Brown S.D., Hettich R.L., Lynd L.R.;
RT   "Profile of Secreted Hydrolases, Associated Proteins, and SlpA in
RT   Thermoanaerobacterium saccharolyticum during the Degradation of
RT   Hemicellulose.";
RL   Appl. Environ. Microbiol. 80:5001-5011(2014).
CC   -!- FUNCTION: Essential cell division protein. {ECO:0000256|HAMAP-
CC       Rule:MF_00910}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00910};
CC       Single-pass type II membrane protein {ECO:0000256|HAMAP-Rule:MF_00910}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane
CC       protein {ECO:0000256|ARBA:ARBA00004606}. Note=Localizes to the division
CC       septum where it forms a ring structure. {ECO:0000256|HAMAP-
CC       Rule:MF_00910}.
CC   -!- SIMILARITY: Belongs to the FtsL family. {ECO:0000256|HAMAP-
CC       Rule:MF_00910}.
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DR   EMBL; CP003184; AFK86569.1; -; Genomic_DNA.
DR   RefSeq; WP_014758439.1; NC_017992.1.
DR   AlphaFoldDB; I3VVM4; -.
DR   STRING; 1094508.Tsac_1562; -.
DR   KEGG; tsh:Tsac_1562; -.
DR   PATRIC; fig|1094508.3.peg.1584; -.
DR   eggNOG; COG2919; Bacteria.
DR   Proteomes; UP000006178; Chromosome.
DR   GO; GO:0032153; C:cell division site; IEA:UniProtKB-UniRule.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00910; FtsL; 1.
DR   InterPro; IPR011922; Cell_div_FtsL.
DR   InterPro; IPR007060; FtsL/DivIC.
DR   NCBIfam; TIGR02209; ftsL_broad; 1.
DR   Pfam; PF04977; DivIC; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_00910};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00910,
KW   ECO:0000313|EMBL:AFK86569.1};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_00910}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00910};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_00910};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_00910}.
FT   TRANSMEM        32..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00910"
FT   COILED          60..90
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   143 AA;  16419 MW;  EEC9488B0BDD97BD CRC64;
     MVLEKHDYDY ELKPYYEENK GKKPKKNRKL KNLAVIVFVG VLSITVLFRY ALIYQKSVAL
     SSVEAKASEI EKLNQQLEVQ IASMSDLQRI EEIAKNQLGM VEPDKGQIVY MSVGKQNQVA
     EKKTDDENRN KTFLGRILGL LVR
//
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