ID A0A1M6PWG7_9FLAO Unreviewed; 458 AA.
AC A0A1M6PWG7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=SAMN05444371_1366 {ECO:0000313|EMBL:SHK12344.1};
OS Epilithonimonas mollis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Epilithonimonas.
OX NCBI_TaxID=216903 {ECO:0000313|EMBL:SHK12344.1, ECO:0000313|Proteomes:UP000184498};
RN [1] {ECO:0000313|Proteomes:UP000184498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18016 {ECO:0000313|Proteomes:UP000184498};
RA Varghese N., Submissions S.;
RL Submitted (NOV-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; FRAM01000001; SHK12344.1; -; Genomic_DNA.
DR RefSeq; WP_072997000.1; NZ_FRAM01000001.1.
DR AlphaFoldDB; A0A1M6PWG7; -.
DR STRING; 216903.SAMN05444371_1366; -.
DR OrthoDB; 9768127at2; -.
DR Proteomes; UP000184498; 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 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}.
FT DOMAIN 7..195
FT /note="SHS2"
FT /evidence="ECO:0000259|SMART:SM00842"
SQ SEQUENCE 458 AA; 50482 MW; 3C7CD18BD56A8A20 CRC64;
MENQEYSVGL DIGTTKIVAI VGRRNAHGKI EILGVGKAKS LGVHKGIVNN ISQTINSIKT
AVAEAQSSAG VPIHKVTVGI AGKHIRSLQH SDYIMREHPD QYITEDDIEK LKDQVKKLVM
LPGEEIIHVL PQEYKVDSEG EIQEPIGMHG KRLEANFHVV VGQMGSIRNI ARCVREAGLE
MEALTLEPLA SSEAVLTKEE KEAGVAIVDI GGGTTDIAIF KDNIIRHTCV IPYGGGIITD
DIKEGCSIIE KHAEQLKVKF GSSVPELEKD STYVTIPGLH GRPDKEISLK VLAQIINARV
EEILEMVNTE LKAYGAFEQK KKLIAGIVLT GGGSNLRNLR QLANYTTGFD SRIGFANEYV
ANDKNQYLKG PEFATSIGLL MESLKIRDKK ILPTEEEIIE EIVTRAEPVA NQPIAETEKI
QIQPIEEIKK VEVAKRNKPT FGQSLMDKVK KFFEEVEE
//
