ID A0A1G4FHN0_9FIRM Unreviewed; 413 AA.
AC A0A1G4FHN0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Cell division protein FtsA {ECO:0000256|HAMAP-Rule:MF_02033, ECO:0000256|PIRNR:PIRNR003101};
GN Name=ftsA_1 {ECO:0000313|EMBL:SCL84835.1};
GN Synonyms=ftsA {ECO:0000256|HAMAP-Rule:MF_02033};
GN ORFNames=PP176A_0717 {ECO:0000313|EMBL:SCL84835.1};
OS Sporanaerobacter sp. PP17-6a.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Sporanaerobacteraceae;
OC Sporanaerobacter.
OX NCBI_TaxID=1891289 {ECO:0000313|EMBL:SCL84835.1, ECO:0000313|Proteomes:UP000179042};
RN [1] {ECO:0000313|EMBL:SCL84835.1, ECO:0000313|Proteomes:UP000179042}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PP176A {ECO:0000313|EMBL:SCL84835.1};
RA Seilhamer J.J.;
RL Submitted (AUG-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}.
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DR EMBL; FMIF01000004; SCL84835.1; -; Genomic_DNA.
DR RefSeq; WP_071139069.1; NZ_FMIF01000004.1.
DR AlphaFoldDB; A0A1G4FHN0; -.
DR Proteomes; UP000179042; 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; 3.30.1490.110; -; 1.
DR Gene3D; 3.30.420.40; -; 1.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000179042}.
FT DOMAIN 5..193
FT /note="SHS2"
FT /evidence="ECO:0000259|SMART:SM00842"
SQ SEQUENCE 413 AA; 45454 MW; 5647A84CBA58F43D CRC64;
MGELITSVDI GTSKVCVIIA EIDKSKQIRI IGVGISPCYG VKKGIVVDIE DTSKAVSYAL
EQAENMADIE VDNAYVNIAG GYTKFTKNKG VIAVSNENRE INSDDVKRVL NSATIISIPQ
NQQIIDIIPL QYIIDGYDEI RDPIGMTGIR LEADVDIVTA SATTVLNIVK SVNGAGLEVL
GIVAEPLATS ESVLTEDEKE LGVLLIDIGA GTTDVSLFKN GSLIYNFLVP IAGNHITNDI
SIGFRIPYKE SEDIKRKYGL NFNPNVNKKR IIEVTPIGSD ERINITNAEL SEIIEARVNE
IIEIIYKELF KRGFVKDILA GIVLTGGGIG YFPKGVDLTK KMFELPVRIG KPDYIGIQEP
IYSTAAGLIN YSLKRKFNYY VEYNNVHNKK TSSKANSNKG LLSFLKKVWE EYF
//
