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Database: UniProt
Entry: B6GCI0_9ACTN
LinkDB: B6GCI0_9ACTN
Original site: B6GCI0_9ACTN 
ID   B6GCI0_9ACTN            Unreviewed;       364 AA.
AC   B6GCI0;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   13-SEP-2023, entry version 46.
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   ORFNames=COLSTE_01803 {ECO:0000313|EMBL:EEA90011.1};
OS   Collinsella stercoris DSM 13279.
OC   Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales;
OC   Coriobacteriaceae; Collinsella.
OX   NCBI_TaxID=445975 {ECO:0000313|EMBL:EEA90011.1, ECO:0000313|Proteomes:UP000003560};
RN   [1] {ECO:0000313|EMBL:EEA90011.1, ECO:0000313|Proteomes:UP000003560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13279 {ECO:0000313|EMBL:EEA90011.1,
RC   ECO:0000313|Proteomes:UP000003560};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Collinsella stercoris (DSM 13279).";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EEA90011.1, ECO:0000313|Proteomes:UP000003560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13279 {ECO:0000313|EMBL:EEA90011.1,
RC   ECO:0000313|Proteomes:UP000003560};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EEA90011.1}.
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DR   EMBL; ABXJ01000105; EEA90011.1; -; Genomic_DNA.
DR   AlphaFoldDB; B6GCI0; -.
DR   STRING; 445975.COLSTE_01803; -.
DR   eggNOG; COG1559; Bacteria.
DR   HOGENOM; CLU_025574_2_2_11; -.
DR   Proteomes; UP000003560; Unassembled WGS sequence.
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   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 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:UP000003560};
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        21..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            252
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ   SEQUENCE   364 AA;  39041 MW;  6498AA49D7DA3F98 CRC64;
     MPQRSQGAYA RGGARPPKKG SPVPVVIGVL IAIAVVAGAA LFLFPRIFGG DSANIEAGQQ
     VSITIPEGSS SDAIATILVD NHIIADSGEY YAAVKKLNAE MSLKPGDYQF ETLQDPLSVV
     KQLVAGPNLE GVKLTVPEGK TVEQTAQLVE DAYGISADEF ISQAKASAYA GDYPFLADAG
     NDSLEGFLYP KTYTFAGTPT ADEVIRAMLD QYQLDVVDAF DFDAGRATIS ATYGIELSDY
     ELLTLASIVE REGLNADQRA HVASVFLNRL AGKGDFAGRP YLQSDATLMY ETGGAVTAED
     IQGIDSPYNS YQNAGLPPTP ICSPSSEAIL ATLEPTDSDD LYFYITQDEE YFSQTYDEHM
     QSWE
//
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