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Database: UniProt
Entry: C3M9B9_SINFN
LinkDB: C3M9B9_SINFN
Original site: C3M9B9_SINFN 
ID   C3M9B9_SINFN            Unreviewed;       395 AA.
AC   C3M9B9;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   27-MAR-2024, entry version 88.
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=NGR_c08950 {ECO:0000313|EMBL:ACP24685.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP24685.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP24685.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT   systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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; CP001389; ACP24685.1; -; Genomic_DNA.
DR   RefSeq; WP_012707469.1; NC_012587.1.
DR   RefSeq; YP_002825438.1; NC_012587.1.
DR   AlphaFoldDB; C3M9B9; -.
DR   STRING; 394.NGR_c08950; -.
DR   KEGG; rhi:NGR_c08950; -.
DR   PATRIC; fig|394.7.peg.3710; -.
DR   eggNOG; COG1559; Bacteria.
DR   HOGENOM; CLU_025574_0_0_5; -.
DR   OrthoDB; 9814591at2; -.
DR   Proteomes; UP000001054; 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:UP000001054};
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        51..77
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   COMPBIAS        1..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            254
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ   SEQUENCE   395 AA;  43151 MW;  38F7D0BCDF686A12 CRC64;
     MSDSNENSAA QFGRNETGSN GPIIPKSANE ALRPERVPEP PKRSRKARSQ VVIFLNFLMT
     VVVFVALAAA GAVYYAMHAY EKPGPLEANQ NFIVRGGAGI IEIAEGLERN NIITDSRVFR
     FVSEAYLDNE TLKAGEYEIK AHASMQEIME LLKSGKSILY AVSLPEGLTV KQMFRKLSDD
     PVLVGDLPAE LPAEGSLKPD TYKFTRGTKR GEIVQQMVSA QKALVSQIWE KRDPELPVTS
     VEEFVTLASI VEKETGRADE RPRVASVFIN RLEKGMRLQS DPTIIYGIFG GEGKPVDRAI
     LKSDLEKETP YNTYLIKGLP PTPIANPGRA ALEAVANPSR TPELYFVADG TGGHVFAATL
     DEHNANVRRW RKLEAEKAAE AAKAAADAAT APEAQ
//
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