ID A0A1E8YIE3_9LACT Unreviewed; 486 AA.
AC A0A1E8YIE3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, entry version 22.
DE RecName: Full=Cell division protein FtsA {ECO:0000256|HAMAP-Rule:MF_02033};
GN Name=ftsA {ECO:0000256|HAMAP-Rule:MF_02033};
GN ORFNames=HMPREF2811_07425 {ECO:0000313|EMBL:OFK55864.1};
OS Globicatella sp. HMSC072A10.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Globicatella.
OX NCBI_TaxID=1739315 {ECO:0000313|EMBL:OFK55864.1, ECO:0000313|Proteomes:UP000176615};
RN [1] {ECO:0000313|EMBL:OFK55864.1, ECO:0000313|Proteomes:UP000176615}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMSC072A10 {ECO:0000313|EMBL:OFK55864.1,
RC ECO:0000313|Proteomes:UP000176615};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-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}.
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}.
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DR EMBL; KV805761; OFK55864.1; -; Genomic_DNA.
DR RefSeq; WP_071408784.1; NZ_KV805761.1.
DR AlphaFoldDB; A0A1E8YIE3; -.
DR OrthoDB; 9768127at2; -.
DR Proteomes; UP000176615; 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; -; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000176615}.
FT DOMAIN 7..194
FT /note="SHS2"
FT /evidence="ECO:0000259|SMART:SM00842"
FT REGION 385..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 486 AA; 54176 MW; 34F81300EA4A2B3D CRC64;
MRNHEIFVSL DIGTTSIKVV VAEYINGQIN IIGVGNVKSR GLSRGVIVDI DETVYSIQQA
VTLAEQKSNV KIKEVSVGIP SNKLGLESCH GMIAVSNENR EITNRDVDNV ITAAKVRSVA
PEREIISVIP EEFVVDGFNG IRDPRGMIGV RLELYATLLT GPRTIIHNIK RCVEKAGLVI
KELVLQPQAI AEVALSQDER EFGTVIIDMG GGQTSASIIY DNQLKYSFVD QEGGDFVTKD
ISIILNTSLE SAERIKREYG YAIASQTSDE EYFPVETVGK KEPVRVDERY LAEIIEARLA
QIFETIHEDL GAVDALDLPG GFVITGGAAS LPGVLELAQK FFGSKVRLFI PEQMGMRNPV
FSTSMGIIEY VAGLDDVHRI AQGTYRPNSR PAQQPEQNHD ASNDYYPAQP NRQTTQYHRP
MSEMSPRTER PRANYDQYQK TSGQENQRYI ENEYYEEETN QGVYEEPSNE NSVASKVKAF
FNTFFD
//
