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Database: UniProt
Entry: B5RBA3_SALG2
LinkDB: B5RBA3_SALG2
Original site: B5RBA3_SALG2 
ID   B5RBA3_SALG2            Unreviewed;       318 AA.
AC   B5RBA3;
DT   04-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   04-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 73.
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=yceG {ECO:0000313|EMBL:CAR37774.1};
GN   Synonyms=mltG {ECO:0000256|HAMAP-Rule:MF_02065};
GN   OrderedLocusNames=SG1923 {ECO:0000313|EMBL:CAR37774.1};
OS   Salmonella gallinarum (strain 287/91 / NCTC 13346).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=550538 {ECO:0000313|EMBL:CAR37774.1, ECO:0000313|Proteomes:UP000008321};
RN   [1] {ECO:0000313|EMBL:CAR37774.1, ECO:0000313|Proteomes:UP000008321}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=287/91 / NCTC 13346 {ECO:0000313|Proteomes:UP000008321};
RX   PubMed=18583645; DOI=10.1101/gr.077404.108;
RA   Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA   Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA   Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA   Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA   Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA   Mungall K., Sanders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA   Humphrey T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT   "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT   gallinarum 287/91 provides insights into evolutionary and host adaptation
RT   pathways.";
RL   Genome Res. 18:1624-1637(2008).
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; AM933173; CAR37774.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5RBA3; -.
DR   KEGG; seg:SG1923; -.
DR   HOGENOM; CLU_025574_0_2_6; -.
DR   Proteomes; UP000008321; 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; 2.
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   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            196
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ   SEQUENCE   318 AA;  36063 MW;  ED61914020BDADC9 CRC64;
     MWKVRHLENS TLLIKNETIF TLKAGTGRLA LGDQLYDEKI INRPRVFQWL LRVEPELSHF
     KAGTYRFTPG MTVREMLELL ESGKEAQFPL RFVEGMRLSD YLKQLREAPY IRHTLPDDDY
     ATVAQALKLA HPEWVEGWFW PDTWMYTANT SDVAILKRAH QKMVKAVDTV WKGRAEGLPY
     KDQNQLVTMA SIIEKETAVA SERDQVASVF INRLRIGMRL QTDPTVIYGM GTSYNGNLSR
     ADLEKPTAYN TYTITGLPPG PIASPSEASL QAAAHPAKTP YLYFVADGKG GHTFNTNLAS
     HNRSVQEYLK VLKEKNGQ
//
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