ID A0A0U3F1P2_9BURK Unreviewed; 98 AA.
AC A0A0U3F1P2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Cell division protein FtsL {ECO:0000256|HAMAP-Rule:MF_00910};
GN Name=ftsL {ECO:0000256|HAMAP-Rule:MF_00910};
GN ORFNames=AT984_14215 {ECO:0000313|EMBL:ALT78168.1};
OS Paucibacter sp. KCTC 42545.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Roseateles.
OX NCBI_TaxID=1768242 {ECO:0000313|EMBL:ALT78168.1, ECO:0000313|Proteomes:UP000056576};
RN [1] {ECO:0000313|EMBL:ALT78168.1, ECO:0000313|Proteomes:UP000056576}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 42545 {ECO:0000313|EMBL:ALT78168.1,
RC ECO:0000313|Proteomes:UP000056576};
RA Kim S.-G., Lee Y.-J.;
RT "Complete genome of Paucibacter sp. KCTC 42545.";
RL Submitted (DEC-2015) 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; CP013692; ALT78168.1; -; Genomic_DNA.
DR RefSeq; WP_058720655.1; NZ_CP013692.1.
DR AlphaFoldDB; A0A0U3F1P2; -.
DR STRING; 1768242.AT984_14215; -.
DR KEGG; pkt:AT984_14215; -.
DR OrthoDB; 5298556at2; -.
DR Proteomes; UP000056576; 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 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.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|HAMAP-Rule:MF_00910};
KW Cell division {ECO:0000256|HAMAP-Rule:MF_00910};
KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00910};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_00910};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00910};
KW Reference proteome {ECO:0000313|Proteomes:UP000056576};
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 REGION 77..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 98 AA; 10823 MW; D34A90FD6E403638 CRC64;
MGRWNLILLL AVLFSGTALV RSAYDARLLF TELDRAQAEG RRLEADGQRL QAERHAQATN
LRVEQVARER LRMHAITPGM SQELDTAPAA AAKPGVSQ
//
