ID A0A223KTI9_9BACI Unreviewed; 378 AA.
AC A0A223KTI9;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=BC6307_15955 {ECO:0000313|EMBL:AST92677.1};
OS Sutcliffiella cohnii.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Sutcliffiella.
OX NCBI_TaxID=33932 {ECO:0000313|EMBL:AST92677.1, ECO:0000313|Proteomes:UP000215224};
RN [1] {ECO:0000313|EMBL:AST92677.1, ECO:0000313|Proteomes:UP000215224}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6307 {ECO:0000313|EMBL:AST92677.1,
RC ECO:0000313|Proteomes:UP000215224};
RA Lee Y.-J., Yi H., Bahn Y.-S., Kim J.F., Lee D.-W.;
RT "The whole genome sequencing and assembly of Bacillus cohnii DSM 6307T
RT strain.";
RL Submitted (DEC-2016) 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}.
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DR EMBL; CP018866; AST92677.1; -; Genomic_DNA.
DR RefSeq; WP_066414863.1; NZ_CP018866.1.
DR AlphaFoldDB; A0A223KTI9; -.
DR STRING; 1314751.GCA_001591425_01784; -.
DR KEGG; bcoh:BC6307_15955; -.
DR Proteomes; UP000215224; 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; 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:UP000215224};
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 29..52
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT SITE 261
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 378 AA; 42828 MW; CC37D7915824471C CRC64;
MAEQRKEKET DIKEKLLEKH HEAKLVRRIV FIVFIILMLS LTAIVAGGYS FVKNSLQPVD
ENAEETTVVE IPIGSSVTAI GNILEENGIV HNAKIFRYYV KFKNESGFQA GEYALSPAMT
LDDIMEELKQ GKIMQEVVFQ VTIPEGRQLT EIATILSNRA NVNEEEFLET VNDPAFVEKM
MARFPVLLTE EILTEDVMYP LEGYLFPATY PFYEENPSIE TIVETMLIKT QEVIIQYSAE
MEEKEMTIHE VLTMASLIEE EATAQTDREN ISSVFYNRLE TGMPLQTDPT IAYALGEHLD
RTLFVHLEVE SPYNTYKYPG LTPGPIANAG ETSIIAALRP AETDYFYFLA TPDGKVLFNR
TLEEHNRDRA THITGSGE
//
