ID A0A077HIW2_9CORY Unreviewed; 375 AA.
AC A0A077HIW2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=CUREI_06655 {ECO:0000313|EMBL:AIL97018.1};
OS Corynebacterium ureicelerivorans.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=401472 {ECO:0000313|EMBL:AIL97018.1, ECO:0000313|Proteomes:UP000028939};
RN [1] {ECO:0000313|EMBL:AIL97018.1, ECO:0000313|Proteomes:UP000028939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMMIB RIV-2301 {ECO:0000313|EMBL:AIL97018.1,
RC ECO:0000313|Proteomes:UP000028939};
RA Tippelt A., Albersmeier A., Brinkrolf K., Ruckert C., Tauch A.;
RT "Complete genome sequence of Corynebacterium ureicelerivorans DSM 45051, a
RT lipophilic and urea-splitting isolate from a blood culture of a septicaemia
RT patient.";
RL Submitted (AUG-2014) 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 -!- SIMILARITY: Belongs to the transglycosylase MltG family.
CC {ECO:0000256|HAMAP-Rule:MF_02065}.
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DR EMBL; CP009215; AIL97018.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A077HIW2; -.
DR STRING; 401472.CUREI_06655; -.
DR KEGG; cuv:CUREI_06655; -.
DR HOGENOM; CLU_025574_4_1_11; -.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000028939; 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 Gene3D; 3.30.1490.480; Endolytic murein transglycosylase; 1.
DR HAMAP; MF_02065; MltG; 1.
DR InterPro; IPR003770; MLTG-like.
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:UP000028939};
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 254
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 375 AA; 40097 MW; B26251A20FE41BA2 CRC64;
MRRTRNTAVL VASLLLIIGL VAWIAITRGS SASDFEGAGN GEEQVVQIQD GASLSELGPE
LADRGIVASD NAFQTAAANN PNADNIQPGF YRLQGEMSAE SAVNALLDPQ QRVTPLQVYG
GATLMDINIL GGQTRLGILS MIQQSACGEK PAADCVNLED LNKAAADADP AALGVPEWAR
EAVGGRAGDA KRLEGLIAPG EYIIDPHASA EEILTDLITR SAKQYDSTDI VGRAKNVGLT
PYELLTAASL VEREAPAGEF DKVARVILNR LDEPMRLEFD STVNYGLPSV EVATTNEDRA
RVTPWNTYAM DGLPQTPIAS PSIEAIEAME NPADGNWLFF VTVDKDGTTI FNDTFEQHLN
DTQRAVDSGV LDSQR
//
