ID A0A0P1G3A1_9RHOB Unreviewed; 442 AA.
AC A0A0P1G3A1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
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 ECO:0000313|EMBL:CUH76104.1};
GN ORFNames=TRN7648_00782 {ECO:0000313|EMBL:CUH76104.1};
OS Tropicibacter naphthalenivorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Tropicibacter.
OX NCBI_TaxID=441103 {ECO:0000313|EMBL:CUH76104.1, ECO:0000313|Proteomes:UP000054935};
RN [1] {ECO:0000313|EMBL:CUH76104.1, ECO:0000313|Proteomes:UP000054935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7648 {ECO:0000313|EMBL:CUH76104.1,
RC ECO:0000313|Proteomes:UP000054935};
RG Swine Surveillance;
RL Submitted (SEP-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; CYSE01000001; CUH76104.1; -; Genomic_DNA.
DR RefSeq; WP_058246293.1; NZ_FWXX01000001.1.
DR AlphaFoldDB; A0A0P1G3A1; -.
DR STRING; 441103.TRN7648_00782; -.
DR OrthoDB; 9810567at2; -.
DR Proteomes; UP000054935; 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; 3.30.420.40; -; 1.
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:UP000054935}.
FT DOMAIN 24..223
FT /note="SHS2"
FT /evidence="ECO:0000259|SMART:SM00842"
SQ SEQUENCE 442 AA; 47685 MW; FDF559A5827E8B1D CRC64;
MIELYESQRA MRNMRKAAMQ RGVVAILDVG SSKIACLVLR FDGTDPSEEG IGSLAGQSGF
RVIGAATTRS RGVRFGEIHS MSETERAIRT AVQAAQKMAG IRVDHVIACF SGAGPRSYGL
AGNVEVQGVT VDEQDVARVL SACDVPDYGH GREVLHAQPV NFALDHRSGL IDPRGQIGNE
LSCDMHMLTV DAQSIQNLAH CVKRCDLELA GLASSAYASG IAALVEDEQE LGAACIDMGG
GATGVSIFIK KHMIFADSVR MGGDHVTQDI SMGLQVPTAT AERIKTFYGG VHATGMDDRE
MIETGGETGD WEHDRRTVSR AELIGIMRPR VEEILEEVKA RLDAAGFEHL PSQKIVLTGA
ASQIPGLDGL ASKMLGQQVR LGRPLRVHGL PQAATGPGFA SAVGLCLFAA HPQDEWWDFE
VPVDRYPARS LKRAVQWFRE NW
//