ID A0A109IHV6_9ACTN Unreviewed; 413 AA.
AC A0A109IHV6;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=GA0070623_5810 {ECO:0000313|EMBL:SCG81431.1};
OS Micromonospora rifamycinica.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=291594 {ECO:0000313|EMBL:SCG81431.1, ECO:0000313|Proteomes:UP000198226};
RN [1] {ECO:0000313|EMBL:SCG81431.1, ECO:0000313|Proteomes:UP000198226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44983 {ECO:0000313|EMBL:SCG81431.1,
RC ECO:0000313|Proteomes:UP000198226};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-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; LT607752; SCG81431.1; -; Genomic_DNA.
DR RefSeq; WP_067312318.1; NZ_LT607752.1.
DR AlphaFoldDB; A0A109IHV6; -.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000198226; 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 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|HAMAP-Rule:MF_02065};
KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_02065};
KW Lyase {ECO:0000256|HAMAP-Rule:MF_02065};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_02065};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_02065};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_02065}.
FT TRANSMEM 47..68
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT SITE 278
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 413 AA; 45265 MW; B8923C90C52DE6E1 CRC64;
MIDDLDLGFD EQERGERGEK GRHRRGFVNR RNGGGSGKSG GGPGKTIFAL LMALVLLGGI
GGGAFYGFDR IRNHFITPDF DGPGTGEALV DVKTGDTATD IGNSLYDAGV VKSTKAFIEA
AEENALSKNI QVGRYKVKKE MRASDALTLL LDPKSRVVNG VTIPEGMITL AIYDLLAKET
KIPVGEFKTA AKDPVKLGVP EFWFNRKDGK KGPRSLEGFL YPATYELPPK ATAAQILSMM
VDKFLDVTEE MKFVETVEAD RGISPYEALI TASIAQAESV NHVDMPKVAR VIYNRVYTDR
YHCKCLEIDS AINYWLRLQG KNPKDSDILK QSELNDPRNP YRTHGADGLT ITPISNPGED
ALKGAMSPPN GTWVYFMTVD KKGTMGYGTT DADFRDLQRQ MCTNGVLSGE NCR
//
