ID A0A0C2VKK4_9BACL Unreviewed; 388 AA.
AC A0A0C2VKK4;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=KP78_34570 {ECO:0000313|EMBL:KIL44493.1};
OS Jeotgalibacillus soli.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Jeotgalibacillus.
OX NCBI_TaxID=889306 {ECO:0000313|EMBL:KIL44493.1, ECO:0000313|Proteomes:UP000031938};
RN [1] {ECO:0000313|EMBL:KIL44493.1, ECO:0000313|Proteomes:UP000031938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P9 {ECO:0000313|EMBL:KIL44493.1,
RC ECO:0000313|Proteomes:UP000031938};
RA Goh K.M., Chan K.-G., Yaakop A.S., Ee R., Gan H.M., Chan C.S.;
RT "Genome sequencing of Jeotgalibacillus soli.";
RL Submitted (JAN-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:KIL44493.1}.
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DR EMBL; JXRP01000019; KIL44493.1; -; Genomic_DNA.
DR RefSeq; WP_041090361.1; NZ_JXRP01000019.1.
DR AlphaFoldDB; A0A0C2VKK4; -.
DR STRING; 889306.KP78_34570; -.
DR PATRIC; fig|889306.3.peg.3474; -.
DR Proteomes; UP000031938; 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:UP000031938};
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 28..51
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT SITE 264
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 388 AA; 44229 MW; D9A5337F0CAE5EEB CRC64;
MSDNQSKIEQ WIHNLQERKK EAKLVRKIVF ISMIVFLLVV VGVGFGGYTY ISSSLEPADP
EDNTAVSVEI PIGSSVDSIV SILEENNIVR DATVFKYYLK FNNESDFQAG TYDLTPSMTL
GEITESLKTG RVYHEPLFMV TVPEGLSLEE IAVIIEENTR FTADEFMTTV DNPEFINSMK
EKYPELVTDS IFGESIQHPL EGYLFPATYP FYDEDQELEE IISQMVEATY VNVTPYIEQY
AETMQNEELT VHDVLTFASL LEEEATEDTD RRLIASVFYN RLEEGMPLQT DPTVLYALGE
WSDRVLFEDL EVDSPYNTYK NTGLPPGPIA SSGVSSIEAV LNPENSNYFY FLASLEDGTV
YYSETLDEHE RKAEEYIYNE REEAETEE
//
