ID A0A1E4IR38_9PROT Unreviewed; 119 AA.
AC A0A1E4IR38;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Cell division protein FtsB {ECO:0000256|HAMAP-Rule:MF_00599};
GN Name=ftsB {ECO:0000256|HAMAP-Rule:MF_00599};
GN ORFNames=ABS91_01735 {ECO:0000313|EMBL:ODU12436.1};
OS Thiobacillus sp. SCN 64-35.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Thiobacillaceae; Thiobacillus.
OX NCBI_TaxID=1660150 {ECO:0000313|EMBL:ODU12436.1, ECO:0000313|Proteomes:UP000094432};
RN [1] {ECO:0000313|EMBL:ODU12436.1, ECO:0000313|Proteomes:UP000094432}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26031303; DOI=10.1111/1462-2920.12936;
RA Kantor R.S., van Zyl A.W., van Hille R.P., Thomas B.C., Harrison S.T.,
RA Banfield J.F.;
RT "Bioreactor microbial ecosystems for thiocyanate and cyanide degradation
RT unravelled with genome-resolved metagenomics.";
RL Environ. Microbiol. 17:4929-4941(2015).
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:ODU12436.1}.
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DR EMBL; MEFJ01000025; ODU12436.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E4IR38; -.
DR Proteomes; UP000094432; 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:ODU12436.1};
KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00599};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00599};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00599};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00599, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00599,
KW ECO:0000256|SAM:Phobius}.
FT TOPO_DOM 1..22
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00599"
FT TRANSMEM 21..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TOPO_DOM 41..119
FT /note="Periplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00599"
SQ SEQUENCE 119 AA; 13170 MW; B3567FB3C03F208F CRC64;
MRSASAANTG WKRLGARLRT HGLAWALGLA IVLLQYPLWL GEGGWLKVHE GAQKIVGQQT
LNHRLQARND GLIAELGDLK QGRDAIEERA RNELGMIAPD EWFVRVVTSH PIQTGKANE
//
