ID A0A0X3APD5_9FLAO Unreviewed; 458 AA.
AC A0A0X3APD5;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=Ga0061079_10348 {ECO:0000313|EMBL:CVK15738.1};
OS Apibacter mensalis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Apibacter.
OX NCBI_TaxID=1586267 {ECO:0000313|EMBL:CVK15738.1, ECO:0000313|Proteomes:UP000182761};
RN [1] {ECO:0000313|EMBL:CVK15738.1, ECO:0000313|Proteomes:UP000182761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R-53146 {ECO:0000313|EMBL:CVK15738.1,
RC ECO:0000313|Proteomes:UP000182761};
RA McClelland M., Jain A., Saraogi P., Mendelson R., Westerman R.,
RA SanMiguel P., Csonka L.;
RL Submitted (JAN-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; FCOR01000003; CVK15738.1; -; Genomic_DNA.
DR RefSeq; WP_055424965.1; NZ_LIVM01000003.1.
DR AlphaFoldDB; A0A0X3APD5; -.
DR STRING; 1586267.GCA_001418685_00570; -.
DR OrthoDB; 9768127at2; -.
DR Proteomes; UP000182761; 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:UP000182761}.
FT DOMAIN 7..195
FT /note="SHS2"
FT /evidence="ECO:0000259|SMART:SM00842"
FT REGION 395..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 458 AA; 50498 MW; A4FB4411AACF29E2 CRC64;
MNDNNIAVGL DIGTTKIVAI VGQRNDHGKL VILGMGRAKS LGVHRGVVNN ITQTIDSIKK
AINEAEKAAN YKITDVTVGI AGQHIRSLQH SDYISRPNFE DVIDDTDIEK LKEQVHKLVM
LPGEEIVHVL PQEYKVDSQS EIIEPRGFHG SRLEANFHVV VGQISLIRNI ARCVKEAGLN
LVGITLEPLA SSDAVLSQEE KEAGVALIDV GGGTTDIAVF KDNIIRHTAV IPFGGNVITD
DIKSGCSIIE RQAEILKVKY GSAWPSENKE IEVISIPGLH GRDPKEITVK KLSQIIHARV
EEIISLAYME LKNYGCEEQK KKLIAGIVMT GGGSKLKHLR QLTEYTTGMD IRIGYCNEHL
AGGQPEELAS PEYATAIGLL MTGLKNLDLK KNKIQQEPKN IKNPEAIAES PNEKNSPNNT
LNIDQKNLNE EKKKNKDKKK SIFASFQEKF IKYINDTE
//
