ID   FTSK_AZOBR     STANDARD;      PRT;   631 AA.
AC   O83045;
DT   10-OCT-2003 (Rel. 42, Created)
DT   10-OCT-2003 (Rel. 42, Last sequence update)
DT   05-JUL-2004 (Rel. 44, Last annotation update)
DE   DNA translocase ftsK (Fragment).
GN   Name=ftsK;
OS   Azospirillum brasilense.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Azospirillum.
OX   NCBI_TaxID=192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Sp7 / ATCC 29145;
RX   MEDLINE=98385818; PubMed=9720864;
RA   de Zamaroczy M.;
RT   "Structural homologues PII and PZ of Azospirillum brasilense provide
RT   intracellular signalling for selective regulation of various nitrogen-
RT   dependent functions.";
RL   Mol. Microbiol. 29:449-463(1998).
CC   -!- FUNCTION: DNA motor protein, which is both required to move DNA
CC       out of the region of the septum during cell division and for the
CC       septum formation. Tracks DNA in an ATP-dependent manner by
CC       generating positive supercoils in front of it and negative
CC       supercoils behind it (By similarity).
CC   -!- SUBUNIT: Homohexamer. This suggests the formation of a ring
CC       between the two cells at the septum that surrounds DNA (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Integral membrane protein. Located at the
CC       septum. The large C-terminal part of the protein is cytoplasmic
CC       (Potential).
CC   -!- SIMILARITY: Contains 1 FtsK domain.
CC   --------------------------------------------------------------------------
CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; X92496; CAA63241.1; -.
DR   HAMAP; MF_01809; -; 1.
DR   InterPro; IPR002543; FtsK_SpoIIIE.
DR   Pfam; PF01580; FtsK_SpoIIIE; 1.
DR   PROSITE; PS50901; FTSK; 1.
KW   ATP-binding; Cell division; Chromosome partition; DNA-binding;
KW   Transmembrane.
FT   TRANSMEM     45     67       Potential.
FT   TRANSMEM     94    116       Potential.
FT   TRANSMEM    128    150       Potential.
FT   TRANSMEM    183    205       Potential.
FT   DOMAIN      478    631       FtsK.
FT   NP_BIND     495    502       ATP (Potential).
FT   NON_TER     631    631
SQ   SEQUENCE   631 AA;  67101 MW;  81CAB67411DE639D CRC64;
     MARPASPRSG SGKSAGARPA GARTEKPPFF SPATRAFVVA RAREMAGFAL GVVGLVLMVI
     LGSYNPADPS WNAVPAADVH IHNLFGRFGA HLADVLIQSL GWAAYLLALV PMMWGWRLSL
     QKSVRHPLFR SVLAVWGVLM VAMFLAGMGT GSEDPLKSRP GGSFGGLLLD GVSRLLFGSP
     GNPLVGTVAG VAGGLILFVA MGLSIREWAA SLRETAAGLA RLGRGARTGL SFVRDKGAEA
     ARSAARQTGG LLRREPSLAT AEKTTAAPTL DDTPDEDGGA ITLRAAPRGR LSDSISVEPR
     VEAKTRAVPV VTSPAGGKTK AADQGRPSKQ AALNLEEADG YELPPLDLLQ IVPTSVRGEK
     VDEAALRENA VKLEGVLSDF GVRGEVQKVH PGPVVTLYEL EPAPGTKSSR VIGLADDIAR
     SMSAVSVRVA VVPGRNVIGI ELPNAKRETV LLRELLAGDV FDKTAGKLLL ALGKDIGGQS
     VVADLARFPH LLVAGTTGSG KSVAINTMIL SLLYRLPPDR CRFIMIDPKM LELSVYEGIP
     HLLTPVVTDP KKAVVALKWT VREMEDRYRN MSKLGVRNIE GYNARLREAR ADGELLTRRV
     QTGFDPDTGK PIFEEQPLDL KELPYIVVIV D
//