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Entry: Q3J794_NITOC
LinkDB: Q3J794_NITOC
Original site: Q3J794_NITOC 
ID   Q3J794_NITOC            Unreviewed;       411 AA.
AC   Q3J794;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 87.
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   OrderedLocusNames=Noc_2856 {ECO:0000313|EMBL:ABA59302.1};
OS   Nitrosococcus oceani (strain ATCC 19707 / BCRC 17464 / JCM 30415 / NCIMB
OS   11848 / C-107).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Nitrosococcus.
OX   NCBI_TaxID=323261 {ECO:0000313|EMBL:ABA59302.1, ECO:0000313|Proteomes:UP000006838};
RN   [1] {ECO:0000313|Proteomes:UP000006838}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19707 / BCRC 17464 / NCIMB 11848 / C-107
RC   {ECO:0000313|Proteomes:UP000006838};
RX   PubMed=16957257; DOI=10.1128/AEM.00463-06;
RA   Klotz M.G., Arp D.J., Chain P.S.G., El-Sheikh A.F., Hauser L.J.,
RA   Hommes N.G., Larimer F.W., Malfatti S.A., Norton J.M., Poret-Peterson A.T.,
RA   Vergez L.M., Ward B.B.;
RT   "Complete genome sequence of the marine, chemolithoautotrophic, ammonia-
RT   oxidizing bacterium Nitrosococcus oceani ATCC 19707.";
RL   Appl. Environ. Microbiol. 72:6299-6315(2006).
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 inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_02033}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_02033}; Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_02033}.
CC       Note=Localizes to the Z ring in an FtsZ-dependent manner. Targeted to
CC       the membrane through a conserved C-terminal amphipathic helix.
CC       {ECO:0000256|HAMAP-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; CP000127; ABA59302.1; -; Genomic_DNA.
DR   RefSeq; WP_002812443.1; NC_007484.1.
DR   AlphaFoldDB; Q3J794; -.
DR   STRING; 323261.Noc_2856; -.
DR   KEGG; noc:Noc_2856; -.
DR   eggNOG; COG0849; Bacteria.
DR   HOGENOM; CLU_037850_3_2_6; -.
DR   InParanoid; Q3J794; -.
DR   Proteomes; UP000006838; 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   CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR   Gene3D; 3.30.1490.110; -; 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}; Cell inner membrane {ECO:0000256|HAMAP-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:UP000006838}.
FT   DOMAIN          10..196
FT                   /note="SHS2"
FT                   /evidence="ECO:0000259|SMART:SM00842"
SQ   SEQUENCE   411 AA;  44350 MW;  391AC9DAD33D93F2 CRC64;
     MSKRSDKNFI VGLDIGTSKI AAIVAETHPE GEIEVVGIGS HPSRGLKKGV VVNIDSTVQS
     IQRAVEEAES MAGCQIYSVF TGIAGSHIRS QNSDGVVPIR DKEVTTEDVE RVIDSARAVA
     IPADQKILHV LPQEFIIDSQ EGIRDPVGMS GVRLEAKVHL VFGAVSAAQN IIKCIRRCGL
     EADDIILQQL ASSYSVLTDD EQELGVCLVD IGGGTTDIAV FVGGAIRHTA VIPIAGDQVT
     NDIAVALRTP TQHADDIKLR YACALTQLTH PDEHIEVPSV GDRPPRRLSR QALAGVIEPR
     YRELLELVME ELQRSGYEEL LGAGVVLTGG SAKMEGVMEL AEEVFHTPVR LGIPQHMAGL
     PDVVRNPVHA TGIGLLLFGH HHPYTPGLGG RPLRSVRGVW DRMRGWFQGN F
//
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