ID A0A1H8BPB2_9BACT Unreviewed; 483 AA.
AC A0A1H8BPB2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=SAMN04487902_10456 {ECO:0000313|EMBL:SEM84710.1};
OS Prevotella sp. ne3005.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1761887 {ECO:0000313|EMBL:SEM84710.1, ECO:0000313|Proteomes:UP000199132};
RN [1] {ECO:0000313|Proteomes:UP000199132}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NE3005 {ECO:0000313|Proteomes:UP000199132};
RA Varghese N., Submissions S.;
RL Submitted (OCT-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}.
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DR EMBL; FOCK01000004; SEM84710.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8BPB2; -.
DR STRING; 1761887.SAMN04487902_10456; -.
DR Proteomes; UP000199132; 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; -; 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; 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:UP000199132}.
FT DOMAIN 8..194
FT /note="SHS2"
FT /evidence="ECO:0000259|SMART:SM00842"
FT REGION 390..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..463
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 483 AA; 54080 MW; 41F357FEFA8429E2 CRC64;
MMAAKEFIVA IELGSSKMTG IAGQKNLDGS INVLAVVKEP SSSFIRKGVV YNIDKTAQCL
TSIVRKLENQ LKTGITQVYV GVGGQSIRGV KNVVSKDLPT ETIISQDMVI ELMDANRNMT
YQDQEILDAA VQEYKVGSQF QLDPVGIQAN RLEGHFLNIL ERKSFYRNLN KCFETANINV
AEMYLAPLAL ADSVLTETEK RSGCALVDIG ADTTTVSVYS KNILRHLAVI PLGSNNITKD
IATLQMEDSD AERMKLKYGS AYTDNNDIDN DLKYSIDSER QIESRKFIEI VEGRMEEIIE
NVWYQIPSEY YDKLLGGIIL TGGGSNMKNI EKAFINHTHV DKIRIAKSIT HTINTTNEEI
KAKNGMLNTV LGLLVKGDIN CAGSAINPNG DLFSSQKQPV HPTADQRPAR QATDTPAGVI
RTEAEKQKAE EEKRRQQEEE ERIKREEELK KKEEEERIRK ENSTWNKLKK GILKFGKSIV
EEE
//
