ID A0A386ZBC8_9NOCA Unreviewed; 495 AA.
AC A0A386ZBC8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, 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=D7D52_11645 {ECO:0000313|EMBL:AYF74404.1};
OS Nocardia yunnanensis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=2382165 {ECO:0000313|EMBL:AYF74404.1, ECO:0000313|Proteomes:UP000267164};
RN [1] {ECO:0000313|EMBL:AYF74404.1, ECO:0000313|Proteomes:UP000267164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFHS0054 {ECO:0000313|EMBL:AYF74404.1,
RC ECO:0000313|Proteomes:UP000267164};
RA Zhang J.;
RT "Nocardia yunnanensis sp. nov., an actinomycete isolated from a soil
RT sample.";
RL Submitted (SEP-2018) 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; CP032568; AYF74404.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A386ZBC8; -.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000267164; 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 Gene3D; 3.30.1490.480; Endolytic murein transglycosylase; 1.
DR HAMAP; MF_02065; MltG; 1.
DR InterPro; IPR003770; MLTG-like.
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 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 121..142
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT REGION 1..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 374
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 495 AA; 53896 MW; 33913A07308B142D CRC64;
MTDRWTRAEE RYRQNAERRY RRDDLDWSQA DDYEDDTTVI PRYEDEHYAD EPYTADEYDE
EPPLAPEPPR RSAPQRAERT RAQGRSGRGQ SRASGGRGGS RPKRSRVASR KAAERKRRRR
NLFVIAGVFA VLFVGAVGFA GWKFVGKLNP PADFSGPQGP LVVIQIKTGD TATQIAQTMA
DKGIVKSSGA FYEAAVRNTN MNSIQPGYYA IPGHSKGSEA VTALFSKDAR VGNVVISEGR
QLHDSSDAST NARKDGIYRK IADASCVGTG TAAKCVTYEA LDQAGATADP ATLGVPTWAL
ERVKSAPDRT RQLEGLIAGG TWDFDPSASA QDILKQLVTA SAQTYEASGL MQSGSANGLS
PYDTLIAASL VEREALPQDM SKVARVIVNR LAAQQKLEFD STVNYNLDKT EVATTDADRA
KKTPWNTYAS PGLPATPISA PSLDATRAME NPAPGNWLYF VTVDKQGTTL FTDNYQAHLS
NIEKARQSGI LDSGR
//
