ID A0A0P0C416_9BACT Unreviewed; 444 AA.
AC A0A0P0C416;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=DC20_01295 {ECO:0000313|EMBL:ALI97857.1};
OS Rufibacter tibetensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Rufibacter.
OX NCBI_TaxID=512763 {ECO:0000313|EMBL:ALI97857.1, ECO:0000313|Proteomes:UP000061382};
RN [1] {ECO:0000313|EMBL:ALI97857.1, ECO:0000313|Proteomes:UP000061382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1351 {ECO:0000313|EMBL:ALI97857.1,
RC ECO:0000313|Proteomes:UP000061382};
RA Dai J.;
RT "Complete genome sequence of Rufibacter tibetensis strain 1351t, a
RT radiation-resistant bacterium from tibet plateau.";
RL Submitted (AUG-2015) 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; CP012643; ALI97857.1; -; Genomic_DNA.
DR RefSeq; WP_062542172.1; NZ_CP012643.1.
DR AlphaFoldDB; A0A0P0C416; -.
DR STRING; 512763.DC20_01295; -.
DR KEGG; rti:DC20_01295; -.
DR PATRIC; fig|512763.3.peg.291; -.
DR OrthoDB; 9768127at2; -.
DR Proteomes; UP000061382; 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 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000061382}.
FT DOMAIN 8..196
FT /note="SHS2"
FT /evidence="ECO:0000259|SMART:SM00842"
SQ SEQUENCE 444 AA; 48456 MW; 3B84E7E772EA26CE CRC64;
MTQNDKIVVG LDIGTTKICA LVGRKNEYGK LEILGLGKAV SEGVVRGMVS NIDKTVEAIR
KAIRQAEEQS GIDIKVVNVG IAGQHIKSLQ HNGSITRTSL DSEITVEDVN RLTNDMYRLV
TPPGSEIIHV MPQDYKVDYE DGIMDPVGMT GVRLEGNFHI ITAQSNAVNN ITKCITRAGL
EIDQLILEPL ASCMSVLSEE EREAGVALID IGGGTTDLAI FKDNIIRHTA VLPFGGNIIT
SDIKQGCMVM QNQAEQLKVR FGKAIADEAS DNEIVSIPGL RDRTPKEISL KNLAFIIEAR
MEEIVELVYS EIVRSGYANQ LAAGVVITGG GAQLQNLVQL VEYLTGLDAR IGYPNEHLGK
SKIDSVKSPM FATTVGLVLA GYQALDERVN RYTEMTNTPE NRVVNEVKPV QKSSGGGGSD
FFKKIFERTK GMLIDDFDDK QQNY
//