ID A4T4Z2_MYCGI Unreviewed; 742 AA.
AC A4T4Z2;
DT 15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 15-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE SubName: Full=Cell division protein FtsK/SpoIIIE {ECO:0000313|EMBL:ABP43256.1};
GN OrderedLocusNames=Mflv_0771 {ECO:0000313|EMBL:ABP43256.1};
OS Mycolicibacterium gilvum (strain PYR-GCK) (Mycobacterium gilvum (strain
OS PYR-GCK)).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350054 {ECO:0000313|EMBL:ABP43256.1};
RN [1] {ECO:0000313|EMBL:ABP43256.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP43256.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Miller C., Richardson P.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABP43256.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP43256.1};
RX PubMed=23469141;
RA Badejo A.C., Badejo A.O., Shin K.H., Chai Y.G.;
RT "A Gene Expression Study of the Activities of Aromatic Ring-Cleavage
RT Dioxygenases in Mycobacterium gilvum PYR-GCK to Changes in Salinity and pH
RT during Pyrene Degradation.";
RL PLoS ONE 8:E58066-E58066(2013).
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DR EMBL; CP000656; ABP43256.1; -; Genomic_DNA.
DR AlphaFoldDB; A4T4Z2; -.
DR STRING; 350054.Mflv_0771; -.
DR KEGG; mgi:Mflv_0771; -.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_003134_1_1_11; -.
DR OrthoDB; 9807790at2; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR CDD; cd01127; TrwB_TraG_TraD_VirD4; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR023836; EccCa-like_Actinobacteria.
DR InterPro; IPR002543; FtsK_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR03924; T7SS_EccC_a; 1.
DR PANTHER; PTHR22683; SPORULATION PROTEIN RELATED; 1.
DR PANTHER; PTHR22683:SF1; TYPE VII SECRETION SYSTEM PROTEIN ESSC; 1.
DR Pfam; PF01580; FtsK_SpoIIIE; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50901; FTSK; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00289}; Cell cycle {ECO:0000313|EMBL:ABP43256.1};
KW Cell division {ECO:0000313|EMBL:ABP43256.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00289}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 41..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 455..664
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT BINDING 478..485
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 742 AA; 80440 MW; 16A6280799A41FD9 CRC64;
MTTRKFTPII KRGPRLTPGE INVAPPEDLG VDIPPSGMQK ALPWVMGGCM LGMIAILIFG
GLRNFSPYML MMPMMVVMGA VGMMASGGSG GKKVPEINAD RKEYLRYLAG LRTRVTSSAA
AQVSFFNYHA PHPDDLLSIV GTHRQWSRAA NHDFYAATRI GLGSEPAVDR LLKPAVGAEL
AGPAGAPQPH LEPVSHMWVT KFLRTHGLIH DCPKLLQLRT FPTIAVGGDT DGAVGLLTAM
ICHLAVFHPP DMLQMRVLTD NPEDPVWAWL KWLPHLQHQT DTDAAGATRM VFTRTDGLSD
LAARGPHTAD ATPSGPYVVV IDLTGGRAGF PMDGRSGVTV LTLGNHRSTY RIRVDAGDGT
ADDKLPGASF RLVASEVDRM SPAQAERLAR KLAGWSITGT IIDKGTRVQK KVATEWHEIV
GAQSVEEVTP ARWRMFTDTD RDRLRIPFGH ELKTGDVMYL DIKEGAEFGA GPHGMLIGTT
GSGKSEFLRT LILSLAATHH PDQINLLLTD FKGGSTFLGM EKLPHTAAVV TNMEEEAELV
SRMGEVLTGE LDRRQSILRQ AGIQVGAAGA LSGVAEYEKH RERGADLPPL PTLFVVVDEF
AELLQNHPDF IGLFDRICRV GRSLRVHLLL ATQSLNTGGT RIDKLEPNLT YRIALRTTSS
AESKAVIGTP EAQYITNKES GVGFLRVGME DPVKFQSVYT GTPYVPVTVG AGDDDTPRAH
ADSGIRIHRF TTAPIADTRV TV
//
