ID U5P2E4_9STRE Unreviewed; 450 AA.
AC U5P2E4;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=N597_01995 {ECO:0000313|EMBL:AGY37728.1};
OS Streptococcus ilei.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1156431 {ECO:0000313|EMBL:AGY37728.1, ECO:0000313|Proteomes:UP000017124};
RN [1] {ECO:0000313|EMBL:AGY37728.1, ECO:0000313|Proteomes:UP000017124}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=I-P16 {ECO:0000313|Proteomes:UP000017124};
RA Hyun D.-W.;
RT "Genome sequence of Streptococcus SP. I-P16 isolated from human ileal
RT fluid.";
RL Submitted (SEP-2013) 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; CP006776; AGY37728.1; -; Genomic_DNA.
DR RefSeq; WP_023022469.1; NZ_QSTR01000003.1.
DR STRING; 1156433.N597_01995; -.
DR KEGG; sip:N597_01995; -.
DR PATRIC; fig|1156433.3.peg.349; -.
DR HOGENOM; CLU_037850_1_1_9; -.
DR Proteomes; UP000017124; Chromosome.
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 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}.
FT DOMAIN 7..194
FT /note="SHS2"
FT /evidence="ECO:0000259|SMART:SM00842"
SQ SEQUENCE 450 AA; 49154 MW; 4CF544D817F15B42 CRC64;
MARNGFFTGL DIGTSSIKVL VAEHVNGEMN VIGVSNAKSA GVKDGIIVDI EAASNAIKNA
VSQAEEKAGI SINLVNVGLP ANLLQIEATQ GMIPVTSDSK EITDADVENV VRSALTKSMT
PDREVITFIP EEFTVDGFQG IRDPRGMMGI RLEMRGLLYT GPRTVLHNLR KTVERAGLQV
ENIIISPLAM IKSVLNEGER EFGATVIDLG GGQTTVASVR NQELQFTNIY QEGGDYVTKD
ISKVLKTSQK LAEGLKFNYG AAYVPAVGDE VFHVEVIGEV EPVQVSEKYL AEIISARIKH
IFDQIKQDLE RRHLLDLPGG IVIIGGGAIL PGIEELAQEV FGVNVKLYVP NQIGIRNPAF
AHVISLSEYA GNLTDVDILA QAAVHGDQRL RQQPIQFERP TQQPVVPAYV PDEIEPVVNV
EQQHPVEEQK QEEKTTFTDR MKNLIGNMFD
//
