ID A0A0M9ZMZ6_9ACTN Unreviewed; 590 AA.
AC A0A0M9ZMZ6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, 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=ADL01_27455 {ECO:0000313|EMBL:KOV65052.1};
OS Streptomyces sp. NRRL WC-3618.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519490 {ECO:0000313|EMBL:KOV65052.1, ECO:0000313|Proteomes:UP000037738};
RN [1] {ECO:0000313|EMBL:KOV65052.1, ECO:0000313|Proteomes:UP000037738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL WC-3618 {ECO:0000313|EMBL:KOV65052.1,
RC ECO:0000313|Proteomes:UP000037738};
RA Noorani M.;
RL Submitted (JUL-2015) 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:KOV65052.1}.
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DR EMBL; LGDW01000393; KOV65052.1; -; Genomic_DNA.
DR RefSeq; WP_053744670.1; NZ_LGDW01000393.1.
DR AlphaFoldDB; A0A0M9ZMZ6; -.
DR PATRIC; fig|1519490.3.peg.5995; -.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000037738; 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 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:UP000037738};
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 236..258
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT REGION 1..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..164
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 466
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 590 AA; 64470 MW; 1C30140DA5A11FF3 CRC64;
MTEYGRGPGS EPWHPEDPLY GDGGWDGQQA QADQSSYGGQ PQHYPQQSQQ PQQQYGDWSA
DGQQAAYGQA QQQYPPQQYQ QQPQHQQYSQ QYGEQSPQQY ADQGQQQYAN GGWDGGQQAQ
VPYPADPTDP YAQQTAAYGG EQADYYGTPD AYPPPEPPAR RRPEPQSQSQ PESEPEPQTD
WDPGPDQGEH AFFAGGDEGD DEPDGEAEGR RGRGERKGRD GGKSGKSGKT KKGRNGTACL
IIVLVFGGGI AGVGYFGYQF YQNRFGPAPD YTGDGTSATV TVEIPKGATG YVIARALEKK
GVVKSVDAFV AAQAENPDGK KIQAGVYVLN KEMSGKSAVA LMLNPKSQNN MIVAPGQRNV
QVYAAIDEKL GLSKGTTAKV AKKDYKSFGL PDWANDNEEI KDPLEGFLYP TTYPAAKGMK
PAAVLKEMVT TATAKYETLD LEAKAKKLDL DSPLEVLTVA SLVQAEGKTS DDYRKMAEVV
YNRLDLGNPQ TYGFLQFDST FNYVKNQSNI DISESEINKN KDPYNTYTKK GLPPGPIGNP
GDVAMKATLN PTDDGWYYFV ATDGVSKTEF AKTHEEFQRL KDKFNASKRS
//
