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Database: UniProt
Entry: A0A1I7ENN3_9BURK
LinkDB: A0A1I7ENN3_9BURK
Original site: A0A1I7ENN3_9BURK 
ID   A0A1I7ENN3_9BURK        Unreviewed;       116 AA.
AC   A0A1I7ENN3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   31-JUL-2019, entry version 7.
DE   RecName: Full=Cell division protein FtsL {ECO:0000256|HAMAP-Rule:MF_00910};
GN   Name=ftsL {ECO:0000256|HAMAP-Rule:MF_00910};
GN   ORFNames=SAMN05192563_103763 {ECO:0000313|EMBL:SFU25521.1};
OS   Paraburkholderia aspalathi.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=1324617 {ECO:0000313|EMBL:SFU25521.1, ECO:0000313|Proteomes:UP000198844};
RN   [1] {ECO:0000313|EMBL:SFU25521.1, ECO:0000313|Proteomes:UP000198844}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 27731 {ECO:0000313|EMBL:SFU25521.1,
RC   ECO:0000313|Proteomes:UP000198844};
RA   de Groot N.N.;
RL   Submitted (OCT-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
CC       cytoplasmic, with the downstream cell division proteins, which are
CC       predominantly 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}. 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; FPBH01000037; SFU25521.1; -; Genomic_DNA.
DR   Proteomes; UP000198844; Unassembled WGS sequence.
DR   GO; GO:0032153; C:cell division site; IEA:UniProtKB-UniRule.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00910; FtsL; 1.
DR   InterPro; IPR011922; Cell_div_FtsL.
DR   PANTHER; PTHR37479; PTHR37479; 1.
DR   Pfam; PF04999; FtsL; 1.
DR   TIGRFAMs; TIGR02209; ftsL_broad; 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:SFU25521.1};
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00910};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00910};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000198844};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00910};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_00910};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00910}.
FT   SIGNAL        1     21       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        22    116       Cell division protein FtsL.
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5011516558.
FT   REGION       87    116       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COILED       33     53       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   116 AA;  12783 MW;  79EE66B0B302FE28 CRC64;
     MSRLNIFLLM IVMGCALSVV NATNQQRQIF IQLQRAQSQE RQLQQDYSQL QYQQSALSKT
     SRIEQIATDS LKMQSVTTGR TQYLTLDPGA AKAEDAPIPT SGPASAPLAT RRGGVR
//
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