ID A0A1M6ALL1_9ACTN Unreviewed; 588 AA.
AC A0A1M6ALL1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=SAMN05444521_7329 {ECO:0000313|EMBL:SHI37352.1};
OS Streptomyces sp. 3214.6.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1882757 {ECO:0000313|EMBL:SHI37352.1, ECO:0000313|Proteomes:UP000190947};
RN [1] {ECO:0000313|Proteomes:UP000190947}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3124.6 {ECO:0000313|Proteomes:UP000190947};
RA Varghese N., Submissions S.;
RL Submitted (NOV-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; LT670819; SHI37352.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M6ALL1; -.
DR STRING; 1882757.SAMN05444521_7329; -.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000190947; Chromosome i.
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; 3.30.1490.480; 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:UP000190947};
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 234..256
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT REGION 1..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 464
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 588 AA; 63746 MW; EBF24D69D67555DC CRC64;
MTEYGRGPGS EPWHPEDPLY GDGGWEGQQA HVGHQPAYGG QQQHHYPQQP QQEYGDWGQG
QAQQYDQQQY DPQYQGYDQQ QYADQSPQQY AHQNQQNHQN HQGYQEGYQE GGWDGTGTHA
HVPYAADPGD PYGQQAAAYG AEQPDFYGTP DAYPPPEPPA RRRPEPEPAQ PEPEPEPEQK
PDWDPGPDQG EHAFFAGGGA EDDEDDDEPE GRGNRRGRGD KGAKGAKSKK SRNGFACLVV
VLVFAGGIGG VGYFGYHYYK NRYGAAPDYA GGGTAQSVSV EVPRGSGGAA IGRLLKEAGV
VKSVDAFVSA FTSNPQAGSI QAGAYILKKE MSAKNAVAMM LDPKSQANVV VAPGQRNVGV
YKLIDTKLGL ASGATRKVAE TEFKKLGLPS WANDNSNIKD PLEGFLFPGT YPAAKGMKPE
AILKAMVAHA NEVYGGYNLD AKAKALKLES PLQVITVASL VQAEGKTHED YRKMAEVVYN
RLKPTNDQTN QLLQFDSSFN YLKGESKIHI SAAEINSNKD PYNTYTNKGL PPGPIGNPGD
DALKATLNPT ADGWIYFVAT DGESNTEFAK TFAEFQKLKD KFDASTGN
//
