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Database: UniProt
Entry: F4A369_MAHA5
LinkDB: F4A369_MAHA5
Original site: F4A369_MAHA5 
ID   F4A369_MAHA5            Unreviewed;       384 AA.
AC   F4A369;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 52.
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=Mahau_1104 {ECO:0000313|EMBL:AEE96302.1};
OS   Mahella australiensis (strain DSM 15567 / CIP 107919 / 50-1 BON).
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacterales Family IV. Incertae Sedis; Mahella.
OX   NCBI_TaxID=697281 {ECO:0000313|EMBL:AEE96302.1, ECO:0000313|Proteomes:UP000008457};
RN   [1] {ECO:0000313|Proteomes:UP000008457}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15567 / CIP 107919 / 50-1 BON
RC   {ECO:0000313|Proteomes:UP000008457};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Teshima H., Brettin T.,
RA   Detter J.C., Han C., Tapia R., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Pukall R.,
RA   Steenblock K., Schneider S., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Mahella australiensis DSM 15567.";
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEE96302.1, ECO:0000313|Proteomes:UP000008457}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15567 / CIP 107919 / 50-1 BON
RC   {ECO:0000313|Proteomes:UP000008457};
RX   PubMed=21886860;
RA   Sikorski J., Teshima H., Nolan M., Lucas S., Hammon N., Deshpande S.,
RA   Cheng J.F., Pitluck S., Liolios K., Pagani I., Ivanova N., Huntemann M.,
RA   Mavromatis K., Ovchinikova G., Pati A., Tapia R., Han C., Goodwin L.,
RA   Chen A., Palaniappan K., Land M., Hauser L., Ngatchou-Djao O.D., Rohde M.,
RA   Pukall R., Spring S., Abt B., Goker M., Detter J.C., Woyke T., Bristow J.,
RA   Markowitz V., Hugenholtz P., Eisen J.A., Kyrpides N.C., Klenk H.P.,
RA   Lapidus A.;
RT   "Complete genome sequence of Mahella australiensis type strain (50-1
RT   BON).";
RL   Stand. Genomic Sci. 4:331-341(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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_02065};
CC       Single-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_02065}.
CC   -!- SIMILARITY: Belongs to the transglycosylase MltG family.
CC       {ECO:0000256|HAMAP-Rule:MF_02065}.
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DR   EMBL; CP002360; AEE96302.1; -; Genomic_DNA.
DR   RefSeq; WP_013780732.1; NC_015520.1.
DR   AlphaFoldDB; F4A369; -.
DR   STRING; 697281.Mahau_1104; -.
DR   KEGG; mas:Mahau_1104; -.
DR   eggNOG; COG1559; Bacteria.
DR   HOGENOM; CLU_025574_2_2_9; -.
DR   OrthoDB; 9814591at2; -.
DR   Proteomes; UP000008457; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; 2.
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 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:UP000008457};
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   TRANSMEM        25..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT   SITE            255
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ   SEQUENCE   384 AA;  43580 MW;  4E2528197DC334DF CRC64;
     MPEIMTDEKQ MNNSLPQPRP WWKKALSQVT IFLISLAIVL GGLTLAGWKL YQHYFGPMAP
     GSDEVIEVEI PLGSSTTKIA NILEENKLVR SATIFRYYVD FSGNSGKLKA GIYKLKPSMT
     MSQMLEEMLT GKAMAATKTF TVVPGSTVES MANSLVKQGL IKDTKRFLEL AKSDEFDTYW
     FIADIENADK RRYKLEGYLY PDTYQVYANA NEEQIITKML DQFEKVFSEE YKQRAQELNM
     TVDQVVTLAS VIEKEAGAKD FAKVSAVFHN RIKKDMPLQS CATISYIKGQ TILFASGSDI
     KIESPYNTYK YKGLPAGPIS NPGKNAIQAA LYPEQSFLDQ YYYFAVSDPD TKETVYSKTL
     KEHNKVVAQY RDVWLEWQKE HSSN
//
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