ID A0A1E8CZD8_9MICO Unreviewed; 412 AA.
AC A0A1E8CZD8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=BA895_14785 {ECO:0000313|EMBL:OFE17745.1};
OS Humibacillus sp. DSM 29435.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Humibacillus.
OX NCBI_TaxID=1869167 {ECO:0000313|EMBL:OFE17745.1, ECO:0000313|Proteomes:UP000175826};
RN [1] {ECO:0000313|Proteomes:UP000175826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29435 {ECO:0000313|Proteomes:UP000175826};
RA Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL Submitted (JUL-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}.
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:OFE17745.1}.
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DR EMBL; MAST01000005; OFE17745.1; -; Genomic_DNA.
DR RefSeq; WP_070190833.1; NZ_MAST01000005.1.
DR AlphaFoldDB; A0A1E8CZD8; -.
DR STRING; 1869167.BA895_14785; -.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000175826; 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:UP000175826};
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 73..94
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 289
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 412 AA; 43238 MW; 9A49BFC95573B44F CRC64;
MTDHLESSIF GEHEDHPDAL PGGHHDAGTD RSPAAAAETE RGSRRGRRSS RRSGRAAGSG
GPRRSRPSLW RRLLVIVLAL AVVGGGVTVA VVVLRPVVEG FLESNDFPGP GEGEVSVTVA
PGSGGSAIAD LLVARGVVKT SKAFNEAAAA DEKSSGIQPG VYKLKEAMKA SDALAVLVDP
ANRVITRVVI PEGLWATEIY AKLSQQTGIP VAKYVAAAKD GAALGLPSSA KGNVEGYLFP
ASYEFEPGSS APDQLQQMVA QSTKRLSALG ITPDKMERVV ILASLVEGEA QTAADRGKVA
RVVENRLARD TPLGFDSTVN YIFKKRGVPT QAMLNSASPY NTRKVKGLPP GPIANPGENA
IKAAAAPPAG DWFWFTTVNL CTGETKFAVS DADNAKNVAQ FRAWYQATDG KC
//
