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Database: UniProt
Entry: Q817Z1_BACCR
LinkDB: Q817Z1_BACCR
Original site: Q817Z1_BACCR 
ID   Q817Z1_BACCR            Unreviewed;       373 AA.
AC   Q817Z1;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   24-JAN-2024, entry version 96.
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=BC_4379 {ECO:0000313|EMBL:AAP11292.1};
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900 {ECO:0000313|EMBL:AAP11292.1, ECO:0000313|Proteomes:UP000001417};
RN   [1] {ECO:0000313|EMBL:AAP11292.1, ECO:0000313|Proteomes:UP000001417}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB
RC   9373 / NCTC 2599 / NRRL B-3711 {ECO:0000313|Proteomes:UP000001417};
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(2003).
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   -!- SIMILARITY: Belongs to the transglycosylase MltG family.
CC       {ECO:0000256|HAMAP-Rule:MF_02065}.
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DR   EMBL; AE016877; AAP11292.1; -; Genomic_DNA.
DR   RefSeq; NP_834091.1; NC_004722.1.
DR   RefSeq; WP_000572132.1; NC_004722.1.
DR   AlphaFoldDB; Q817Z1; -.
DR   KEGG; bce:BC4379; -.
DR   PATRIC; fig|226900.8.peg.4529; -.
DR   HOGENOM; CLU_025574_2_3_9; -.
DR   OMA; AVNKYQR; -.
DR   Proteomes; UP000001417; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
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 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:UP000001417};
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   SITE            240
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ   SEQUENCE   373 AA;  42019 MW;  944000A7DF5CFEDF CRC64;
     MIENQVKKKR RRIFLFSIIA LLLVCGSVYA YISSALGPVD SGNKKEIEVE IPKGSSTSKI
     GEILEEKGAV KNGTVFSFYT KAKSKSLQAG TYLLNPSMNA EDVIEQMSAG NVHRPALYKV
     TIKEGAQVTE IAETIATELK WNKDDVTRQL NDKAFIQKMQ QKYPKLLTDK IFDSNIKYPL
     EGYLYPATYS FYKKDTTLEE IVIPMLEKTN AIIVQNEAKM KAKNWDVHQL LTLSSLIEEE
     ATGFTDRQKI SSVFYNRLAK GMPLQTDPTV LYALGKHKQR VLYEDLKVNS PYNTYVVKGL
     PVGPIANSGK HSVEAALEPA QTDYYYFLAA PSGEVYYAKT LEEHNALKQK YITKKTVKWG
     GIAKKVAHPS FLW
//
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