ID A0A1M7PT93_9BURK Unreviewed; 91 AA.
AC A0A1M7PT93;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Cell division protein FtsL {ECO:0000256|HAMAP-Rule:MF_00910};
GN Name=ftsL {ECO:0000256|HAMAP-Rule:MF_00910};
GN ORFNames=SAMN05192549_105376 {ECO:0000313|EMBL:SHN20700.1};
OS Duganella sacchari.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Duganella.
OX NCBI_TaxID=551987 {ECO:0000313|EMBL:SHN20700.1, ECO:0000313|Proteomes:UP000184339};
RN [1] {ECO:0000313|EMBL:SHN20700.1, ECO:0000313|Proteomes:UP000184339}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sac-22 {ECO:0000313|EMBL:SHN20700.1,
RC ECO:0000313|Proteomes:UP000184339};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Essential cell division protein. May link together the
CC upstream cell division proteins, which are predominantly cytoplasmic,
CC with the downstream cell division proteins, which are predominantly
CC periplasmic. {ECO:0000256|HAMAP-Rule:MF_00910}.
CC -!- SUBUNIT: Part of a complex composed of FtsB, FtsL and FtsQ.
CC {ECO:0000256|HAMAP-Rule:MF_00910}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_00910}; Single-pass type II membrane protein
CC {ECO:0000256|HAMAP-Rule:MF_00910}. Membrane
CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606}. Note=Localizes to the division septum
CC where it forms a ring structure. {ECO:0000256|HAMAP-Rule:MF_00910}.
CC -!- SIMILARITY: Belongs to the FtsL family. {ECO:0000256|HAMAP-
CC Rule:MF_00910}.
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DR EMBL; FRCX01000005; SHN20700.1; -; Genomic_DNA.
DR RefSeq; WP_072785254.1; NZ_FRCX01000005.1.
DR AlphaFoldDB; A0A1M7PT93; -.
DR STRING; 551987.SAMN05192549_105376; -.
DR OrthoDB; 5298556at2; -.
DR Proteomes; UP000184339; Unassembled WGS sequence.
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 NCBIfam; TIGR02209; ftsL_broad; 1.
DR PANTHER; PTHR37479; CELL DIVISION PROTEIN FTSL; 1.
DR PANTHER; PTHR37479:SF1; CELL DIVISION PROTEIN FTSL; 1.
DR Pfam; PF04999; FtsL; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:SHN20700.1};
KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00910};
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 COILED 27..54
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 91 AA; 10331 MW; 82ECAADAF7E5E030 CRC64;
MSNKVNLVLT ILLVACGLSL VNAQYQARHL FIELERAQSQ ARQLDIEWAQ LQLDQSTLGK
HARIEEIARR DLNMTPLTAA RTQYLTPEAT K
//
