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Database: UniProt/TrEMBL
Entry: Q39YL6_GEOMG
LinkDB: Q39YL6_GEOMG
Original site: Q39YL6_GEOMG 
ID   Q39YL6_GEOMG            Unreviewed;       627 AA.
AC   Q39YL6;
DT   22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2005, sequence version 1.
DT   24-JAN-2024, entry version 125.
DE   RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00047, ECO:0000256|HAMAP-Rule:MF_00911};
DE   Includes:
DE     RecName: Full=D-alanine--D-alanine ligase {ECO:0000256|HAMAP-Rule:MF_00047};
DE              EC=6.3.2.4 {ECO:0000256|HAMAP-Rule:MF_00047};
DE     AltName: Full=D-Ala-D-Ala ligase {ECO:0000256|HAMAP-Rule:MF_00047};
DE     AltName: Full=D-alanylalanine synthetase {ECO:0000256|HAMAP-Rule:MF_00047};
DE   Includes:
DE     RecName: Full=Cell division protein FtsQ {ECO:0000256|HAMAP-Rule:MF_00911};
GN   Name=ddl {ECO:0000256|HAMAP-Rule:MF_00047,
GN   ECO:0000313|EMBL:ABB30658.1};
GN   Synonyms=ftsQ {ECO:0000256|HAMAP-Rule:MF_00911,
GN   ECO:0000313|EMBL:ABB30658.1};
GN   OrderedLocusNames=Gmet_0415 {ECO:0000313|EMBL:ABB30658.1};
OS   Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15).
OC   Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=269799 {ECO:0000313|EMBL:ABB30658.1, ECO:0000313|Proteomes:UP000007073};
RN   [1] {ECO:0000313|EMBL:ABB30658.1, ECO:0000313|Proteomes:UP000007073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 53774 / DSM 7210 / GS-15
RC   {ECO:0000313|Proteomes:UP000007073};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Geobacter metallireducens GS-15.";
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABB30658.1, ECO:0000313|Proteomes:UP000007073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 53774 / DSM 7210 / GS-15
RC   {ECO:0000313|Proteomes:UP000007073};
RX   PubMed=19473543; DOI=10.1186/1471-2180-9-109;
RA   Aklujkar M., Krushkal J., DiBartolo G., Lapidus A., Land M.L., Lovley D.R.;
RT   "The genome sequence of Geobacter metallireducens: features of metabolism,
RT   physiology and regulation common and dissimilar to Geobacter
RT   sulfurreducens.";
RL   BMC Microbiol. 9:109-109(2009).
CC   -!- FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00047}.
CC   -!- FUNCTION: Essential cell division protein. {ECO:0000256|HAMAP-
CC       Rule:MF_00911}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) +
CC         phosphate; Xref=Rhea:RHEA:11224, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57416,
CC         ChEBI:CHEBI:57822, ChEBI:CHEBI:456216; EC=6.3.2.4;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00047};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00047}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00911}; Single-pass type II membrane protein
CC       {ECO:0000256|HAMAP-Rule:MF_00911}. Cytoplasm
CC       {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|HAMAP-Rule:MF_00047}.
CC       Note=Localizes to the division septum. {ECO:0000256|HAMAP-
CC       Rule:MF_00911}.
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000256|ARBA:ARBA00010871, ECO:0000256|HAMAP-Rule:MF_00047}.
CC   -!- SIMILARITY: Belongs to the FtsQ/DivIB family. FtsQ subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00911}.
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DR   EMBL; CP000148; ABB30658.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q39YL6; -.
DR   STRING; 269799.Gmet_0415; -.
DR   KEGG; gme:Gmet_0415; -.
DR   eggNOG; COG1181; Bacteria.
DR   eggNOG; COG1589; Bacteria.
DR   HOGENOM; CLU_436005_0_0_7; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000007073; Chromosome.
DR   GO; GO:0032153; C:cell division site; IEA:UniProtKB-UniRule.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0090529; P:cell septum assembly; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-UniRule.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   Gene3D; 3.40.50.11690; Cell division protein FtsQ/DivIB; 1.
DR   Gene3D; 3.10.20.310; membrane protein fhac; 1.
DR   HAMAP; MF_00047; Dala_Dala_lig; 1.
DR   HAMAP; MF_00911; FtsQ_subfam; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR005548; Cell_div_FtsQ/DivIB_C.
DR   InterPro; IPR000291; D-Ala_lig_Van_CS.
DR   InterPro; IPR005905; D_ala_D_ala.
DR   InterPro; IPR011095; Dala_Dala_lig_C.
DR   InterPro; IPR011127; Dala_Dala_lig_N.
DR   InterPro; IPR026579; FtsQ.
DR   InterPro; IPR045335; FtsQ_C_sf.
DR   InterPro; IPR034746; POTRA.
DR   InterPro; IPR013685; POTRA_FtsQ_type.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   NCBIfam; TIGR01205; D_ala_D_alaTIGR; 1.
DR   PANTHER; PTHR23132; D-ALANINE--D-ALANINE LIGASE; 1.
DR   PANTHER; PTHR23132:SF23; D-ALANINE--D-ALANINE LIGASE B; 1.
DR   Pfam; PF07478; Dala_Dala_lig_C; 1.
DR   Pfam; PF01820; Dala_Dala_lig_N; 1.
DR   Pfam; PF03799; FtsQ_DivIB_C; 1.
DR   Pfam; PF08478; POTRA_1; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS00843; DALA_DALA_LIGASE_1; 1.
DR   PROSITE; PS00844; DALA_DALA_LIGASE_2; 1.
DR   PROSITE; PS51779; POTRA; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409};
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW   Rule:MF_00911};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW   Rule:MF_00911}; Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00911};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_00911};
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW   Rule:MF_00047};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW   ECO:0000256|HAMAP-Rule:MF_00047};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00047};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00047};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00911};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW   Rule:MF_00047}; Reference proteome {ECO:0000313|Proteomes:UP000007073};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_00911};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_00911}.
FT   DOMAIN          107..303
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          418..486
FT                   /note="POTRA"
FT                   /evidence="ECO:0000259|PROSITE:PS51779"
SQ   SEQUENCE   627 AA;  68402 MW;  5037F39115EEAC7C CRC64;
     MTRDELKTKK IGVLMGGLSA EREISLSSGG AVHKALLARG YDAVAIDVDR DLPQVLVREW
     IDVAFICLHG RYGEDGAVQG VLELMGIPYT GSGVLASALA MNKIFAKQAF AAAGLTITPH
     RVLVRGETFD AVAAGIDLPV VVKPSQEGSS VGVSIVKKAE ELAAALEAAF RYDNEILVEK
     FVKGREIQVG ILDDRAMGAI EIVPKKEFYD FEAKYTDGMA EHICPPVLPA DLYRKLLAEG
     EKAHRALGCA GYSRVDFLVT EGGDCFLLEV NTLPGMTALS LLPEIAQKEA GIAFEELVER
     ILVSASLKIQ GPGTGDRVQK NTRNHRGNAG RGAGCLFLPV PGPWSPITDF MRDLHVKTRI
     QPANKSRNRV KKERKPINWR PLITWGSRAV LGALAVAVVG GAGYKGYAFA SRYEIAVLQV
     EAIEVSKLRH LTRDEVLGQA GVRRGDSMLG LRLRRIGEQL AKNPWIEKVQ VRRYFPHTIR
     IEVVEREPVA VVNMGFLYYL DAKGEVFKPL TQGDSLNFPV ITGITEDDLA RDPKGAREML
     TGAVALMDML KKGRAFTLAD VSEVHIDKGF GLTLFTAGGG VPVRLGKDGY ETKLARFATV
     YGELKTQMTA VEYIDCDYQD KIIVKKG
//
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