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Database: UniProt
Entry: L0KR01_MESAW
LinkDB: L0KR01_MESAW
Original site: L0KR01_MESAW 
ID   L0KR01_MESAW            Unreviewed;       423 AA.
AC   L0KR01;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 50.
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   OrderedLocusNames=Mesau_04802 {ECO:0000313|EMBL:AGB47125.1};
OS   Mesorhizobium australicum (strain HAMBI 3006 / LMG 24608 / WSM2073).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=754035 {ECO:0000313|EMBL:AGB47125.1, ECO:0000313|Proteomes:UP000010998};
RN   [1] {ECO:0000313|Proteomes:UP000010998}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 24608 / HAMBI 3006 / WSM2073
RC   {ECO:0000313|Proteomes:UP000010998};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Gu W., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Reeve W.G., Howieson J.G., Tiwari R.P.,
RA   O'Hara G.W., Atkins C.A., Ronson C.W., Nandasena K.G., Woyke T.;
RT   "Complete sequence of Mesorhizobium australicum WSM2073.";
RL   Submitted (FEB-2012) 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}.
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DR   EMBL; CP003358; AGB47125.1; -; Genomic_DNA.
DR   AlphaFoldDB; L0KR01; -.
DR   STRING; 754035.Mesau_04802; -.
DR   KEGG; mam:Mesau_04802; -.
DR   eggNOG; COG1559; Bacteria.
DR   HOGENOM; CLU_025574_0_0_5; -.
DR   OrthoDB; 9814591at2; -.
DR   Proteomes; UP000010998; Chromosome.
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:UP000010998};
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        49..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          376..423
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        395..409
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            252
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ   SEQUENCE   423 AA;  44966 MW;  D00D7D1A5E256D29 CRC64;
     MNTNPSGNGE FGQRPANTGP IVPKTASEAL RPEAGTPPPK RSRASRSQVV VFMNFVISAV
     MLIVLAAGVA LYFGKQEFTE PGPSANGDTF LVKPSTGVQD IADQLERRGL ISDARVFRLG
     VRAFGNDSAL KAGEYEIKPR ASMRDIMELL KSGKSVMYSL TIPEGLTVEQ ALQRIADEPA
     LSGDMPAKTP PEGSLATDTL RFTRGATRQQ MVDKLLADQK KLVDEVWQRR SPDLPLASVE
     DFVTLASIVE KETGKGDERS RVAAVFLNRL AKGMRLQSDP TIIYGLFGGK GKPADRPIYQ
     SDIQKQTPYN TYVISGLPPT PIANPGRAAL EAVANPSKTD DLYFVADGTG GHVFASTLNE
     HNENVARYRA LQKKQADEAA KAAAAAGASG SADKPADDKP ADEKPAIDSG IDGDAGGDAG
     AAQ
//
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