ID A0A2U2HJY4_9BURK Unreviewed; 108 AA.
AC A0A2U2HJY4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Cell division protein FtsB {ECO:0000256|HAMAP-Rule:MF_00599};
GN Name=ftsB {ECO:0000256|HAMAP-Rule:MF_00599};
GN ORFNames=C7C56_014035 {ECO:0000313|EMBL:PWF47783.1};
OS Massilia glaciei.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1524097 {ECO:0000313|EMBL:PWF47783.1, ECO:0000313|Proteomes:UP000241421};
RN [1] {ECO:0000313|EMBL:PWF47783.1, ECO:0000313|Proteomes:UP000241421}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B448-2 {ECO:0000313|EMBL:PWF47783.1,
RC ECO:0000313|Proteomes:UP000241421};
RA Wang H.;
RT "Massilia violaceinigra sp. nov., a novel purple-pigmented bacterium
RT isolated from Tianshan glacier, Xinjiang, China.";
RL Submitted (APR-2018) 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_00599}.
CC -!- SUBUNIT: Part of a complex composed of FtsB, FtsL and FtsQ.
CC {ECO:0000256|HAMAP-Rule:MF_00599}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_00599}; Single-pass type II membrane protein
CC {ECO:0000256|HAMAP-Rule:MF_00599}. Note=Localizes to the division
CC septum. {ECO:0000256|HAMAP-Rule:MF_00599}.
CC -!- SIMILARITY: Belongs to the FtsB family. {ECO:0000256|HAMAP-
CC Rule:MF_00599}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PWF47783.1}.
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DR EMBL; PXWF02000229; PWF47783.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U2HJY4; -.
DR OrthoDB; 7061211at2; -.
DR Proteomes; UP000241421; 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_00599; FtsB; 1.
DR InterPro; IPR023081; Cell_div_FtsB.
DR InterPro; IPR007060; FtsL/DivIC.
DR PANTHER; PTHR37485; CELL DIVISION PROTEIN FTSB; 1.
DR PANTHER; PTHR37485:SF1; CELL DIVISION PROTEIN FTSB; 1.
DR Pfam; PF04977; DivIC; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|HAMAP-Rule:MF_00599};
KW Cell division {ECO:0000256|HAMAP-Rule:MF_00599,
KW ECO:0000313|EMBL:PWF47783.1};
KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00599};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00599};
KW Coiled coil {ECO:0000256|HAMAP-Rule:MF_00599};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00599};
KW Reference proteome {ECO:0000313|Proteomes:UP000241421};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00599};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00599}.
FT TOPO_DOM 1..3
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00599"
FT TOPO_DOM 22..108
FT /note="Periplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00599"
FT COILED 29..56
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00599"
SQ SEQUENCE 108 AA; 11685 MW; 03A82A92603B0D79 CRC64;
MRIITLALAA LLLLIQFPLW LGKGGKLRVV DLEAKVVEAQ QKTVALRARN AKLESEVRDL
KDGTGAVEER ARYELGMIKQ NEIFVQVLGN KPAVTSVTPA PAPAPAAK
//