GenomeNet

Database: UniProt
Entry: E4RY37_LEAB4
LinkDB: E4RY37_LEAB4
Original site: E4RY37_LEAB4 
ID   E4RY37_LEAB4            Unreviewed;       345 AA.
AC   E4RY37;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Endolytic murein transglycosylase {ECO:0000256|HAMAP-Rule:MF_02065};
DE            EC=4.2.2.- {ECO:0000256|HAMAP-Rule:MF_02065};
DE   AltName: Full=Peptidoglycan polymerization terminase {ECO:0000256|HAMAP-Rule:MF_02065};
GN   Name=mltG {ECO:0000256|HAMAP-Rule:MF_02065};
GN   OrderedLocusNames=Lbys_0602 {ECO:0000313|EMBL:ADQ16365.1};
OS   Leadbetterella byssophila (strain DSM 17132 / JCM 16389 / KACC 11308 / NBRC
OS   106382 / 4M15).
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC   Leadbetterella.
OX   NCBI_TaxID=649349 {ECO:0000313|EMBL:ADQ16365.1, ECO:0000313|Proteomes:UP000007435};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17132;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Teshima H., Brettin T., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B.,
RA   Pomrenke H.G., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Leadbetterella byssophila DSM 17132.";
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADQ16365.1, ECO:0000313|Proteomes:UP000007435}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17132 / JCM 16389 / KACC 11308 / NBRC 106382 / 4M15
RC   {ECO:0000313|Proteomes:UP000007435};
RX   PubMed=21475582; DOI=10.4056/sigs.1413518;
RA   Abt B., Teshima H., Lucas S., Lapidus A., Del Rio T.G., Nolan M., Tice H.,
RA   Cheng J.F., Pitluck S., Liolios K., Pagani I., Ivanova N., Mavromatis K.,
RA   Pati A., Tapia R., Han C., Goodwin L., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Goker M., Tindall B.J.,
RA   Detter J.C., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Leadbetterella byssophila type strain
RT   (4M15).";
RL   Stand. Genomic Sci. 4:2-12(2011).
CC   -!- FUNCTION: Functions as a peptidoglycan terminase that cleaves nascent
CC       peptidoglycan strands endolytically to terminate their elongation.
CC       {ECO:0000256|HAMAP-Rule:MF_02065}.
CC   -!- SIMILARITY: Belongs to the transglycosylase MltG family.
CC       {ECO:0000256|HAMAP-Rule:MF_02065}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002305; ADQ16365.1; -; Genomic_DNA.
DR   RefSeq; WP_013407417.1; NC_014655.1.
DR   AlphaFoldDB; E4RY37; -.
DR   STRING; 649349.Lbys_0602; -.
DR   KEGG; lby:Lbys_0602; -.
DR   eggNOG; COG1559; Bacteria.
DR   HOGENOM; CLU_025574_2_0_10; -.
DR   OrthoDB; 9814591at2; -.
DR   Proteomes; UP000007435; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0008932; F:lytic endotransglycosylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd08010; MltG_like; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR   Gene3D; 3.30.1490.480; Endolytic murein transglycosylase; 1.
DR   HAMAP; MF_02065; MltG; 1.
DR   InterPro; IPR003770; MLTG-like.
DR   NCBIfam; TIGR00247; endolytic transglycosylase MltG; 1.
DR   PANTHER; PTHR30518:SF2; ENDOLYTIC MUREIN TRANSGLYCOSYLASE; 1.
DR   PANTHER; PTHR30518; UNCHARACTERIZED; 1.
DR   Pfam; PF02618; YceG; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_02065};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_02065};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW   ECO:0000256|HAMAP-Rule:MF_02065};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_02065};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_02065};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007435};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_02065};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_02065}.
FT   SITE            221
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ   SEQUENCE   345 AA;  39715 MW;  1A2E43B75A2B6B96 CRC64;
     MTKKRKLFTH FLVLFSTVAA SFAFYLWQVY SSPNLNVDGK ETFVLYIPEG SDYNQVLDSL
     RSHNIIHNEI AFGFLTKRKG YREEIKAGRY EIPPNSSNNT IISKLLAGRQ DPVKLTFNNI
     RTKEDLVRKI GSRLAFNGEE LLAKLQDEDT ANKYGFKSET FMNMFLPDTY FIYWTVTPDA
     FLDRMHSEYK KFWTEERKAK AESIALSPDQ VGILASIVQS ETNKKDEMPV VAGVYMNRLR
     IGMPLQADPT VKFAVGDFSL KRILHKHLSI DSPYNTYKNT GLPPGPIALP ERVALDAVLN
     YQKHNYTYFS AKEDFSGYHN FAENFNEHIK NAQRYQTALN QRGIR
//
DBGET integrated database retrieval system