ID A0A117KD97_9ACTN Unreviewed; 613 AA.
AC A0A117KD97;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=ADL25_00550 {ECO:0000313|EMBL:KUJ58751.1};
OS Streptomyces sp. NRRL F-5122.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1609098 {ECO:0000313|EMBL:KUJ58751.1, ECO:0000313|Proteomes:UP000054048};
RN [1] {ECO:0000313|Proteomes:UP000054048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL F-5122 {ECO:0000313|Proteomes:UP000054048};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (OCT-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:KUJ58751.1}.
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DR EMBL; LMWH01000001; KUJ58751.1; -; Genomic_DNA.
DR RefSeq; WP_059125551.1; NZ_LMWH01000001.1.
DR AlphaFoldDB; A0A117KD97; -.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000054048; 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:UP000054048};
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 257..278
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT REGION 1..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 486
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 613 AA; 66785 MW; 961A0E0E5E2B3C68 CRC64;
MTEYGRGQGS APWHPEDPLY GDGGWGGHEG QAPQPPYGGQ PQQHPEQPQQ HYGDWGSAPQ
AGYDQGQQGY QQYPQPGQQQ YPQHGQPQYP QGGQPQYPQP GQQQYPQAGQ QHGQPQYPQP
GQQQYPQPGQ QQYPQPGQPY GQQQGQQYPG QAQQGHGNAG WDPSGQSGAP YANGPSAPYG
SEQPDFYQTP DAYPPPEPPN RRRAEPEPET DWDPGPDRGE HAFFAGGDAD DDADDEAADG
RKGRGDKGTG KKRRNGCACL AVVLVLGGGV GGVGYVGYQF YQSHFGPAPD YEGEGNGQQV
AVTIPQGATG SVIGQVLKKA GVVKSVDAFV AAQEQNSAGK SIQAGTYTLN KQMSAAAAVE
LMLSPRSKNN LIIAEGWRNT KIYTAIDERL KLKAGTTAGV AKKEWKSFGL PDWANSDKAI
QDPLEGFLYP SSYPVAKGMK PEDVLKQMVD LAKEKYAALG IQAKAESLNL ENPLQVLTVA
SLVQAEGKYK HDFEKVATVV YNRLKPDNTE TYGLLDFDST VNYLRGQSKL DTGSVDALRQ
INNPYNTYKF KGLPPGPIDN PGDVAIKAAL KPAKGNWYYF VSINENETLF AETNEEQNRN
RDKYLEEQKK KNQ
//
