ID A0A3S0N3F3_9BURK Unreviewed; 336 AA.
AC A0A3S0N3F3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 13-SEP-2023, entry version 12.
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 ECO:0000313|EMBL:RTZ47968.1};
GN ORFNames=EKL30_03035 {ECO:0000313|EMBL:RTZ47968.1};
OS Candidimonas sp. SYP-B2681.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Candidimonas.
OX NCBI_TaxID=2497686 {ECO:0000313|EMBL:RTZ47968.1, ECO:0000313|Proteomes:UP000288599};
RN [1] {ECO:0000313|EMBL:RTZ47968.1, ECO:0000313|Proteomes:UP000288599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SYP-B2681 {ECO:0000313|EMBL:RTZ47968.1,
RC ECO:0000313|Proteomes:UP000288599};
RA Zhang M.-Y., Zhang Y.-X.;
RT "Candidimonas lamiisoli sp. nov., a novel bacterium can accelerate seed
RT germination.";
RL Submitted (DEC-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 inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_02065}; Single-pass membrane protein {ECO:0000256|HAMAP-
CC 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:RTZ47968.1}.
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DR EMBL; RYDV01000001; RTZ47968.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S0N3F3; -.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000288599; 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; 3.30.160.60; Classic Zinc Finger; 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 inner membrane {ECO:0000256|HAMAP-Rule:MF_02065};
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:UP000288599};
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 7..30
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT SITE 218
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 336 AA; 37657 MW; F82010FFF474B203 CRC64;
MTKLKLIFLY LLLLAAVIAT GLSAVAWYWV EHPVAMDSER IDYIVEAGSR PRSIAQVMNK
SGIHINETAF VALARLTGRD KLLKAGAYEA MRGDTPRVLL ERMANGDMSQ TQITLIEGWT
YQRVRQALRE NPRIRQTMTT LTDAELLSRL GSSASSPEGL FYPDTYVFNP GSSDFDILRR
AYHAQEQLLE SAWAQRDPDL PLKTPYEALV LASIIEKETG HSSDRDRVSG VFINRLRLNM
PLQTDPTVIY GMGEAYQGRI RKKDLQTDTP WNTYTRGGLP PTPIANAGRA ALTAALHPEK
HKFLYFVSRG DGTSEFSQNL LDHNRAVSKY ILGRGN
//
