ID A0A249T469_9BACT Unreviewed; 471 AA.
AC A0A249T469;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
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:ASZ14715.1};
GN ORFNames=CK934_29095 {ECO:0000313|EMBL:ASZ14715.1};
OS Chitinophaga sp. MD30.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=2033437 {ECO:0000313|EMBL:ASZ14715.1, ECO:0000313|Proteomes:UP000217148};
RN [1] {ECO:0000313|EMBL:ASZ14715.1, ECO:0000313|Proteomes:UP000217148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD30 {ECO:0000313|EMBL:ASZ14715.1,
RC ECO:0000313|Proteomes:UP000217148};
RA Wan X., Darris M., Hou S., Donachie S.P.;
RT "Draft genome sequence of a novel Chitinophaga sp., MD30, isolated from a
RT biofilm in an air conditioner condensate pipe.";
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}.
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DR EMBL; CP023254; ASZ14715.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A249T469; -.
DR OrthoDB; 9768127at2; -.
DR Proteomes; UP000217148; 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 Gene3D; 3.30.1490.110; -; 1.
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:UP000217148}.
FT DOMAIN 8..197
FT /note="SHS2"
FT /evidence="ECO:0000259|SMART:SM00842"
FT REGION 412..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 471 AA; 51935 MW; F5B95D4F9A171C56 CRC64;
MNQEAPIIVG LDIGTTKIAA IAGRKNEYGK LEILGFGKAP SFGVQHGMVL NIDQTIKAIR
QALENCYASN PNLEINEVYV GIAGHHIKSL QTRGDIVRND TDAEISQKDI DQLINDQYKT
VIPASDQIID VIPQQYIVDS LQNITYPIGM SGVKVGANFH IITGDKNAIR NINRSVEKSG
LKIRDLVLQP LASAAAVMCD MDFEAGVAIV DIGGGTTDLA VFYEGILKHT AVIPYGGENI
TNDIKNGLGV LKTQAEQMKV QFGYALADEA KNNAYITIPG LRGQSPKEIS VKNLAHIIQA
RMSEILDFVV YHLKQIGMDN KMLNGGIILT GGGSQLKHLI QLTEYTTGVN ARIGYPNEHL
ASGHIDELTK PMYATCVGLI LKGYNDFEND RRALEENYVK INTSYIAKEQ AAQAASTDDQ
WEQQEEEETL PTPEQIQDRK VKERNASLKS FLDRMKTKII DMFTEEEDTK L
//
