ID A0A1H8XGC0_9SPHI Unreviewed; 446 AA.
AC A0A1H8XGC0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
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=SAMN05428947_113177 {ECO:0000313|EMBL:SEP38919.1};
OS Mucilaginibacter sp. OK283.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=1881049 {ECO:0000313|EMBL:SEP38919.1, ECO:0000313|Proteomes:UP000199509};
RN [1] {ECO:0000313|EMBL:SEP38919.1, ECO:0000313|Proteomes:UP000199509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK283 {ECO:0000313|EMBL:SEP38919.1,
RC ECO:0000313|Proteomes:UP000199509};
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; FODR01000013; SEP38919.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8XGC0; -.
DR STRING; 1881049.SAMN05428947_113177; -.
DR OrthoDB; 9768127at2; -.
DR Proteomes; UP000199509; 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; 2.
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 14..202
FT /note="SHS2"
FT /evidence="ECO:0000259|SMART:SM00842"
SQ SEQUENCE 446 AA; 48695 MW; 729D8841C00421D2 CRC64;
MDKSSTQEKS SPIVVGLDIG TTKICVIVGR RSKNGKIEVL GIGKAESAGV TRGMVSNIDK
TVQGITQAVD IAGAQSNVDI KVVFVGIAGQ HIKSLQHRGL ITRRDLQSEI SRKDIDKLIE
DMYNLVMPPG EDIIHVLPQE FTVDNEPGIK DPIGMAGVRL EANFHIISGQ VTAIKNIVKC
VNKANLDSQD LILEPLASSE SVLSEEEKEA GVVLVDIGGG TTDVAIFHEG IIRHTAVIPF
GGNSVTEDIR EGCSVMRNIA EQLKVRFGSA LADENKENEI VCVPGLRGRE PKEISVKNLA
YVIQARMEEI VEHVYYEIKS SGYEKKLIAG IVITGGGAQL KHLRQLVEFV TGLDCRVGYP
TEHLAKNEVL PKNIYEELQS PTFATGIGLL IKGIQKTEYM SVDVPVEKAQ KTKFEGKGKE
GGLFDRLLKK SITFIKDDIN DEDFLK
//
