ID A0A498DSV2_9BACI Unreviewed; 371 AA.
AC A0A498DSV2;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-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:RLL48007.1};
GN ORFNames=D8M04_01635 {ECO:0000313|EMBL:RLL48007.1};
OS Oceanobacillus piezotolerans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=2448030 {ECO:0000313|EMBL:RLL48007.1, ECO:0000313|Proteomes:UP000270219};
RN [1] {ECO:0000313|EMBL:RLL48007.1, ECO:0000313|Proteomes:UP000270219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YLB-02 {ECO:0000313|EMBL:RLL48007.1,
RC ECO:0000313|Proteomes:UP000270219};
RA Yu L.;
RT "Oceanobacillus sp. YLB-02 draft genome.";
RL Submitted (OCT-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}.
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:RLL48007.1}.
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DR EMBL; RCHR01000001; RLL48007.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498DSV2; -.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000270219; 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:UP000270219};
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 27..50
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT SITE 258
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 371 AA; 41770 MW; 1C1153E7E971D085 CRC64;
MSKNNNKGSF KDNLIARSEE ATKVRKIASV IILAILLLII VGGVSGYLYI KSALEPVDPN
NGEEIIVEIP LGSSSSNIAS ILEESGVIKN ATIFQLYIKL NNYSDFQAGN YTLTQSMSLD
EIAENIQEGK VLQEPIYRVT IPEGLTIEQM ADIYAEKLPF TKEEFLEVVN NEDYINELIK
RYSVLTEDIL QEDILVPLEG YLFAATYDFY EEEPTVESVI EQMLSQTELI VSNYLAAIEE
RGLTIHEAVT LSSLVEKEAS NEEQRKQIAG VFYNRLEEGM KLQTDPTVAY AIGEHLQTTL
YEHLEEDSPY NTYMIEGLPI GPISNFSASS LDAVVNPMDS DYLYFLHDAQ GNIHYAETNE
EHNQNRAEYL N
//
