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Database: UniProt
Entry: A0A0E3Y8Y8_9ENTR
LinkDB: A0A0E3Y8Y8_9ENTR
Original site: A0A0E3Y8Y8_9ENTR 
ID   A0A0E3Y8Y8_9ENTR        Unreviewed;       105 AA.
AC   A0A0E3Y8Y8;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   16-JAN-2019, entry version 14.
DE   RecName: Full=Cell division protein FtsL {ECO:0000256|HAMAP-Rule:MF_00910};
GN   Name=ftsL {ECO:0000256|HAMAP-Rule:MF_00910,
GN   ECO:0000313|EMBL:AKC60310.1};
GN   ORFNames=BOBLI757_135 {ECO:0000313|EMBL:AKC60310.1};
OS   Blochmannia endosymbiont of Camponotus (Colobopsis) obliquus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX   NCBI_TaxID=1505597 {ECO:0000313|EMBL:AKC60310.1};
RN   [1] {ECO:0000313|EMBL:AKC60310.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=757 {ECO:0000313|EMBL:AKC60310.1};
RX   PubMed=25861561;
RA   Williams L.E., Wernegreen J.J.;
RT   "Genome evolution in an ancient bacteria-ant symbiosis: parallel gene
RT   loss among Blochmannia spanning the origin of the ant tribe
RT   Camponotini.";
RL   PeerJ 3:E881-E881(2015).
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; CP010049; AKC60310.1; -; Genomic_DNA.
DR   RefSeq; WP_046304627.1; NZ_CP010049.1.
DR   EnsemblBacteria; AKC60310; AKC60310; BOBLI757_135.
DR   KEGG; ben:BOBLI757_135; -.
DR   PATRIC; fig|1505597.4.peg.131; -.
DR   KO; K03586; -.
DR   OrthoDB; 1803426at2; -.
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:AKC60310.1};
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00910};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00910};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00910};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_00910};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00910}.
FT   TRANSMEM     22     42       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00910}.
SQ   SEQUENCE   105 AA;  12421 MW;  8B17575B7B15BB55 CRC64;
     MLYERYDLVK IIKSDLFFYG KYSLILLVLI EIVSLLIVLT TYQTKQLIMD QEQIMLEKEA
     LDIEYRHLII EENVLGNNNR VEHIALNDLQ MQYINPASEN ICIMP
//
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