ID A0A1M3KHM2_9CHLR Unreviewed; 412 AA.
AC A0A1M3KHM2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Cell division protein FtsA {ECO:0000256|HAMAP-Rule:MF_02033, ECO:0000256|PIRNR:PIRNR003101};
GN Name=ftsA {ECO:0000256|HAMAP-Rule:MF_02033};
GN ORFNames=BGO78_17600 {ECO:0000313|EMBL:OJX47282.1};
OS Chloroflexi bacterium 44-23.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1895927 {ECO:0000313|EMBL:OJX47282.1, ECO:0000313|Proteomes:UP000184201};
RN [1] {ECO:0000313|EMBL:OJX47282.1, ECO:0000313|Proteomes:UP000184201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=44-23 {ECO:0000313|EMBL:OJX47282.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cell division protein that is involved in the assembly of the
CC Z ring. May serve as a membrane anchor for the Z ring.
CC {ECO:0000256|HAMAP-Rule:MF_02033, ECO:0000256|PIRNR:PIRNR003101}.
CC -!- SUBUNIT: Self-interacts. Interacts with FtsZ. {ECO:0000256|HAMAP-
CC Rule:MF_02033}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_02033};
CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_02033};
CC Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_02033}. Note=Localizes to
CC the Z ring in an FtsZ-dependent manner. Targeted to the membrane
CC through a conserved C-terminal amphipathic helix. {ECO:0000256|HAMAP-
CC Rule:MF_02033}.
CC -!- SIMILARITY: Belongs to the FtsA/MreB family. {ECO:0000256|HAMAP-
CC Rule:MF_02033, ECO:0000256|PIRNR:PIRNR003101}.
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:OJX47282.1}.
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DR EMBL; MKUW01000006; OJX47282.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M3KHM2; -.
DR STRING; 1895927.BGO78_17600; -.
DR Proteomes; UP000184201; Unassembled WGS sequence.
DR GO; GO:0032153; C:cell division site; IEA:UniProtKB-UniRule.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-UniRule.
DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR HAMAP; MF_02033; FtsA; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR020823; Cell_div_FtsA.
DR InterPro; IPR003494; SHS2_FtsA.
DR NCBIfam; TIGR01174; ftsA; 1.
DR PANTHER; PTHR32432:SF4; CELL DIVISION PROTEIN FTSA; 1.
DR PANTHER; PTHR32432; CELL DIVISION PROTEIN FTSA-RELATED; 1.
DR Pfam; PF14450; FtsA; 1.
DR Pfam; PF02491; SHS2_FTSA; 1.
DR PIRSF; PIRSF003101; FtsA; 1.
DR SMART; SM00842; FtsA; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW Rule:MF_02033};
KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW Rule:MF_02033};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_02033};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_02033}.
FT DOMAIN 6..192
FT /note="SHS2"
FT /evidence="ECO:0000259|SMART:SM00842"
SQ SEQUENCE 412 AA; 43978 MW; 37507AA089805745 CRC64;
MEEPIVVGID IGTTKVCTLI GRIEGDRIIR ILGVGIEPSQ GIRKGSIVDL GAASQAIARS
IEKAQRSCGL EVSDAQVSLA GSHISSVNNR GVAAVSGGMI DVNDMRRALE AAQAVNIPHN
REIIHVIQRG FIVDGQDGIR SPIGMHGFRL EVEAHMITAA AATVENIRQS VEGAGVNVNQ
FVLNPLASAE VVLSETERNM GAIVCDIGGG TTDLAIYIDG DVWHTMVLAV GGNHITSDIA
HGLRLPMDEA EKVKIKYGHA IKEEVGEDQM FTVKSFGDES MIQIPRRDLA HIIEARVEEI
FELVFQEIKR SGYDGLLPAG MVLTGGSSLL PGIRPLASKI LGLPVRLSRP ENLVGLVDQL
NSPAFSTSVG LLYFALAMNE STMPARGGRF VSKVGGSDLL SRVLDFLKKI SP
//
