ID A0A1G1SRC4_9BACT Unreviewed; 469 AA.
AC A0A1G1SRC4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=BEN47_19320 {ECO:0000313|EMBL:OGX81179.1};
OS Hymenobacter lapidarius.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1908237 {ECO:0000313|EMBL:OGX81179.1, ECO:0000313|Proteomes:UP000176294};
RN [1] {ECO:0000313|EMBL:OGX81179.1, ECO:0000313|Proteomes:UP000176294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCM 8643 {ECO:0000313|EMBL:OGX81179.1,
RC ECO:0000313|Proteomes:UP000176294};
RA Sedlacek I., Kralova S., Kyrova K., Maslanova I., Stankova E., Vrbovska V.,
RA Nemec M., Bartak M., Svec P., Busse H.-J., Pantucek R.;
RT "Hymenobacter coccineus sp. nov., Hymenobacter lapidarius sp. nov. and
RT Hymenobacter glacialis sp. nov., isolated from Antarctic soil.";
RL Submitted (AUG-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}.
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:OGX81179.1}.
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DR EMBL; MDZB01000167; OGX81179.1; -; Genomic_DNA.
DR RefSeq; WP_070730872.1; NZ_MDZB01000167.1.
DR AlphaFoldDB; A0A1G1SRC4; -.
DR STRING; 1908237.BEN47_19320; -.
DR OrthoDB; 9768127at2; -.
DR Proteomes; UP000176294; 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; 3.30.420.40; -; 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}.
FT DOMAIN 7..194
FT /note="SHS2"
FT /evidence="ECO:0000259|SMART:SM00842"
SQ SEQUENCE 469 AA; 50230 MW; 31889FDEB6714429 CRC64;
MQQDKIVVGL DIGTTKICAL VGRKNEFGKL EILGMGKAVS EGVSRGIVLN IDKTVDAIKR
AIRQAEEQSG ISIGLVNVGI AGQHIKSLQH NGSITRNSAD TIGPDDVNRL TQDMYRLVTQ
PGSQIIHVMP QDYKVDYEEG IADPVGYEGV RLEGNFHIIT AQSTAINNIN KCVTKAGLEI
ADLILEPLAS SMSILSEEEK EAGVALIDIG GGTTDLAVFK DGIIRHAAVL PFGGNIITQD
IKAGCNVAPG QAEQLKVKFG KAIAEEASDH EIVSIPGLPN RPPKEVSLKN LAYIIEARMS
EIMELVYAEI YRMGLHDKLS AGIVLTGGGS QLQNLEQLTE YITGLDTRIG YPNQHLGKSR
IEAVKSPMYA TTVGLVLSGY HSLDERNSRA PYEQEEQAVP AYYAPQAAAP VATPAPVAET
RASVPVAAAA APTPAPAKPK EPGAASRFFK DIITRTKGLL IDDYDDKSY
//
