ID F7RSZ9_9GAMM Unreviewed; 411 AA.
AC F7RSZ9;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 39.
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=SOHN41_03487 {ECO:0000313|EMBL:EGM68339.1};
OS Shewanella sp. HN-41.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=327275 {ECO:0000313|EMBL:EGM68339.1, ECO:0000313|Proteomes:UP000002956};
RN [1] {ECO:0000313|EMBL:EGM68339.1, ECO:0000313|Proteomes:UP000002956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HN-41 {ECO:0000313|EMBL:EGM68339.1,
RC ECO:0000313|Proteomes:UP000002956};
RX PubMed=21868804; DOI=10.1128/JB.05578-11;
RA Kim D.H., Jiang S., Lee J.H., Cho Y.J., Chun J., Choi S.H., Park H.S.,
RA Hur H.G.;
RT "Draft Genome Sequence of Shewanella sp. Strain HN-41, Which Produces
RT Arsenic-Sulfide Nanotubes.";
RL J. Bacteriol. 193:5039-5040(2011).
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:EGM68339.1}.
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DR EMBL; AFOZ01000043; EGM68339.1; -; Genomic_DNA.
DR RefSeq; WP_007651244.1; NZ_AFOZ01000043.1.
DR AlphaFoldDB; F7RSZ9; -.
DR STRING; 327275.SOHN41_03487; -.
DR OrthoDB; 9810567at2; -.
DR Proteomes; UP000002956; 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; 3.30.1490.110; -; 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}.
FT DOMAIN 10..196
FT /note="SHS2"
FT /evidence="ECO:0000259|SMART:SM00842"
SQ SEQUENCE 411 AA; 44549 MW; FC79028D166735BB CRC64;
MTKNQDRNLI VGLDIGTSKV AVIIGEVLPD GEISIVGLGN HPSRGMDKGG VNDLDSIVRS
VQRALDQAEL MADCQVSSVY LSISGKHIAC QNENGMVSIN DEEVTQEDVD NVIHTARSVK
IPTERRILHV LPQEYAIDVQ DGIRSPIGMS GMRMEAKVHI VTCANDMAKN ITKSVERCGL
KVDDLVFSGI ASADAVLTFD EKDLGVCIVD IGGGTTDIAV YTNGALRHCA VVPVAGNQVT
NDIAKIFRTP SSHAEQIKVQ FACARSSMVS REDSIEVPSV GGRPSRSMSR HTLAEVVEPR
YQELFELVLK ELKDSGLEDQ IAAGIVLTGG TASIQGVVDI AEATFGMPVR VASPLPIKGL
YEYVDQSIYS TGVGLLHYGA RRVIERQFER PERQGVTSAW NRVQSWFKGE F
//
