ID A0A2G1MKW6_9RHOB Unreviewed; 442 AA.
AC A0A2G1MKW6;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, 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 ECO:0000313|EMBL:PHP29399.1};
GN ORFNames=CJ301_02750 {ECO:0000313|EMBL:PHP29399.1};
OS Limimaricola cinnabarinus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Limimaricola.
OX NCBI_TaxID=1125964 {ECO:0000313|EMBL:PHP29399.1, ECO:0000313|Proteomes:UP000221860};
RN [1] {ECO:0000313|EMBL:PHP29399.1, ECO:0000313|Proteomes:UP000221860}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XM1 {ECO:0000313|EMBL:PHP29399.1,
RC ECO:0000313|Proteomes:UP000221860};
RA Ma R., Wang J., Wang Q., Ma Z., Li J., Chen L.;
RT "Draft Genome Sequence of Loktanella cinnabarina Strain XM1, Isolated from
RT Coastal Surface Water.";
RL Submitted (AUG-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PHP29399.1}.
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DR EMBL; NQWH01000003; PHP29399.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G1MKW6; -.
DR OrthoDB; 9810567at2; -.
DR Proteomes; UP000221860; 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}.
FT DOMAIN 24..223
FT /note="SHS2"
FT /evidence="ECO:0000259|SMART:SM00842"
SQ SEQUENCE 442 AA; 47621 MW; 95F384E4296773C8 CRC64;
MGQLYQTQRA MRHMRKAAMQ RGVIAILDVG TSKIACLVLR FDGDAPALDG VGSMAGQSNF
RIIGAATTRS RGVSFGEVAA MAETERAIRT AVQAAQKMAG VRVDHVIATL SGARPRSYGL
DGEVEVEGGQ VTGSDIGRVL AACEMPDYGD GREVLHAQPV NFALDHRSGL ADPRGQIGQR
LTTDMHLLTV DATAIENLLY CIKRCDLEVA GLASSAYVSG VSSLVEDEQE LGAACIDMGG
GSTGISVFIR KHMIYADSVR MGGDHVTSDI SMGLQVPMAT AERIKTFYGG VVATGMDDRE
MIEIGGDTGD WEHDRRTVSR AELIGIMRPR VEEILEEVRQ RLDAAGFEHL PSQQIVLTGG
GSQIPGLDGL ATRILGQQVR LGRPLRVQGL PQAATGPAFA GSVGLCLFAA HPQDEWWDFE
VPAERHSARS FKRAFKWFKD NW
//
