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
//