ID A0A1G6DKX5_9STRE Unreviewed; 455 AA.
AC A0A1G6DKX5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-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 {ECO:0000256|HAMAP-Rule:MF_02033};
GN ORFNames=SAMN02910293_02281 {ECO:0000313|EMBL:SDB45813.1};
OS Streptococcus henryi.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=439219 {ECO:0000313|EMBL:SDB45813.1, ECO:0000313|Proteomes:UP000182508};
RN [1] {ECO:0000313|EMBL:SDB45813.1, ECO:0000313|Proteomes:UP000182508}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A-4 {ECO:0000313|EMBL:SDB45813.1,
RC ECO:0000313|Proteomes:UP000182508};
RA de Groot N.N.;
RL Submitted (OCT-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; FMXP01000042; SDB45813.1; -; Genomic_DNA.
DR RefSeq; WP_018165558.1; NZ_FMXP01000042.1.
DR AlphaFoldDB; A0A1G6DKX5; -.
DR STRING; 439219.SAMN02910293_02281; -.
DR eggNOG; COG0849; Bacteria.
DR Proteomes; UP000182508; 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; IPR021873; FtsA_C.
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; PF11983; FtsA_C; 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:UP000182508}.
FT DOMAIN 7..194
FT /note="SHS2"
FT /evidence="ECO:0000259|SMART:SM00842"
SQ SEQUENCE 455 AA; 49726 MW; 081E5131183A925A CRC64;
MARNGFFTGL DIGTSSIKVL VAEFVSGEMN VIGVSNVPST GVKDGIIVDI EAAAEAIKSA
VKQAEEKAGI TIDKVNVGLP ANLLQIEPTQ GMIPVPSESK EIKDEDVDSV VKSALTKSIT
PEREVISLVP EEFIVDGFQG IRDPRGMMGI RLEMRGLIYT GPSTILHNLR KTVERAGIVV
ENIVISPLAM TKSVLNEGER EFGATVIDMG GGQTTVASMR AQELQYTNIY PEGGEYITKD
ISKVLKTSMQ IAEALKFNFG RADLEEASRS ETVKVDVVGS DQPIDVSEYY LAEIISARIK
HILERVKQDL ERGRLLDLPG GIILIGGGAI MPGVVELAQE IFGTKVKLYV PNQVGIRNPM
FANVISIVEY VGMMSEVDVI SQRAVSGEEL LRRKPVEFGM VKERVVPMFN EKVEQPVVPA
QNFQEQNQPV YNPEPKEQKP KLGERVRGIL GSMFD
//
