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Database: UniProt
Entry: K8B072_9ENTR
LinkDB: K8B072_9ENTR
Original site: K8B072_9ENTR 
ID   K8B072_9ENTR            Unreviewed;       340 AA.
AC   K8B072;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   24-JAN-2024, entry version 31.
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=BN134_446 {ECO:0000313|EMBL:CCJ79740.1};
OS   Cronobacter dublinensis 1210.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Cronobacter.
OX   NCBI_TaxID=1208656 {ECO:0000313|EMBL:CCJ79740.1, ECO:0000313|Proteomes:UP000009342};
RN   [1] {ECO:0000313|EMBL:CCJ79740.1, ECO:0000313|Proteomes:UP000009342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1210 {ECO:0000313|EMBL:CCJ79740.1,
RC   ECO:0000313|Proteomes:UP000009342};
RX   PubMed=23166675; DOI=10.1371/journal.pone.0049455;
RA   Joseph S., Desai P., Ji Y., Cummings C.A., Shih R., Degoricija L., Rico A.,
RA   Brzoska P., Hamby S.E., Masood N., Hariri S., Sonbol H., Chuzhanova N.,
RA   McClelland M., Furtado M.R., Forsythe S.J.;
RT   "Comparative analysis of genome sequences covering the seven cronobacter
RT   species.";
RL   PLoS ONE 7:e49455-e49455(2012).
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}.
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:CCJ79740.1}.
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DR   EMBL; CAKZ01000019; CCJ79740.1; -; Genomic_DNA.
DR   AlphaFoldDB; K8B072; -.
DR   Proteomes; UP000009342; Unassembled WGS sequence.
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            218
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ   SEQUENCE   340 AA;  38436 MW;  004352E8B1A1E2D0 CRC64;
     MKKMLRVALL LVLVLAVAAG VGYWKVRQLA HSPLPIAKDT IFTLKPGTGR LALGQQLYDE
     KLIKRPRVFQ WLLRLEPELS HFKAGTYRFT PKMTVRDALR LLASGKEAQF PLRFVEGMKL
     SDWLKQLREA PYIKHTLKDD EYATVAQALK LEHPDWVEGW FWPDTWLYTA NTSDVALLKR
     AHQRMVKAVD DVWKSRMDGL PYSSPNQLVT MASIIEKETA VASERDRVAS VFINRLRIGM
     RLQTDPTVIY GMGKSYNGKL TRKDLETPTP YNTYVISGLP PGPIAMPGEA SLKAAAHPAK
     TPYLYFVADG KGGHTFTTNL ASHNRAVQDY LKALKDKNEQ
//
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