ID A0A1M6VE66_9ACTN Unreviewed; 908 AA.
AC A0A1M6VE66;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=SAMN05421803_1348 {ECO:0000313|EMBL:SHK79738.1};
OS Nocardiopsis flavescens.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Nocardiopsis.
OX NCBI_TaxID=758803 {ECO:0000313|EMBL:SHK79738.1, ECO:0000313|Proteomes:UP000184452};
RN [1] {ECO:0000313|EMBL:SHK79738.1, ECO:0000313|Proteomes:UP000184452}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.5723 {ECO:0000313|EMBL:SHK79738.1,
RC ECO:0000313|Proteomes:UP000184452};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
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; FQZK01000034; SHK79738.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M6VE66; -.
DR STRING; 758803.SAMN05421803_1348; -.
DR Proteomes; UP000184452; 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 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:UP000184452};
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 565..584
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT REGION 1..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..344
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..446
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..463
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..520
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..558
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 784
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 908 AA; 97499 MW; 7A35C060742AC060 CRC64;
MNDRDDYSDN PYRGRADRDG GHDYDPLDGP PARGRRSRAE GSPWAEPEEP GSRHTGPSTG
EFRTPRYAPR PDQEYDPLTP RRPARGQEPP AAPQRRGGAA DALRGGRAAR SGGGRGGRPR
ENGPGDAGPP PADDSTQDAL AALAGLGSPA PSPAGEEPPR RARRERPEPE QAPPAPADEE
PRAARRGRRS AEEETPRRGR ANAEEEPPRR GRGRKRGRRD EEPGFLDGLP EDTGAFDAVA
FPGVNSSADT GAFAALTDED LRSRGARGGD APDSGSFDST PRRGRRHRGG AAEEAPEPVE
ESRRSGRRRR GPAEEAPSDT GAFEADAPPR GRRARRDRAP GADPRDTGSY ETGSYDTGSY
DTAAFDTGPR GAGPRSSGGH DTGSYDTGSY DTGAFPDGGD TADGGAPDAA EEEQPRSRRS
RRSRAADEPA QAPRSRRRRG AAPDEVPEEE AEPAEAEFSA EDEDDEPAGR RGRGRGRRAG
TRRGGRQRGR REEESAPAAD EPAAEESGDD GYDDYEEPAL SDIAEAYGGG RDSRRKAKEL
KRARLAQQQR TPEGRRAKRR GKGMTIFLVL VLIAVIGGGG FFVMRTYVFP PDFDGEGSGD
VVYVIQDSQS GASVGQGLAD LGVVASPRAF TNALEDLSAE ELGQGLVPGS YSLALGMSAD
NAVRALLDPA NRLGGRVTIN EGRRNEQVLE QLSEETGVPY EELEEAHSRP DELGLPDYAE
GEAAGYLFPS TYMFDPDTDA ETMLKTMVQQ FHATAEELEL ESRAEALGLT PDEVMAIASI
VQAESGNTDD MPKVSRVVYN RLDIDMNLRM DSTCFYAIGE YGIALNNEQL ARCQADTSGF
DTYHKSGLPP GPFVAPGEDA IEAALSPAEG DWLFFVATDP ENGVTEFTAS ETEFEQLKQE
FMDNWSGG
//
