ID K2JDK3_9RHOB Unreviewed; 388 AA.
AC K2JDK3;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, 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=B30_07211 {ECO:0000313|EMBL:EKE72752.1};
OS Celeribacter baekdonensis B30.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Celeribacter.
OX NCBI_TaxID=1208323 {ECO:0000313|EMBL:EKE72752.1, ECO:0000313|Proteomes:UP000006762};
RN [1] {ECO:0000313|EMBL:EKE72752.1, ECO:0000313|Proteomes:UP000006762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B30 {ECO:0000313|EMBL:EKE72752.1,
RC ECO:0000313|Proteomes:UP000006762};
RA Wang W.;
RT "Celeribacter baekdonensis B30 Genome Sequencing.";
RL Submitted (SEP-2012) 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}.
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:EKE72752.1}.
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DR EMBL; AMRK01000003; EKE72752.1; -; Genomic_DNA.
DR RefSeq; WP_009571387.1; NZ_AMRK01000003.1.
DR AlphaFoldDB; K2JDK3; -.
DR STRING; 1208323.B30_07211; -.
DR PATRIC; fig|1208323.3.peg.1491; -.
DR eggNOG; COG1559; Bacteria.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000006762; 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; 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:UP000006762};
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 263
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 388 AA; 42192 MW; 476F325171D12270 CRC64;
MWRSIASNAL TLLIVVLIAF AGVIAWGKRE YTAAGPLEQA VCLRVPSGST MRRVSDDLAS
KGAISYPSIF RIGADYSDKA QQLKAGSFLV PEGASMAQIT DLITRGGAST CGTEVVYRIG
VNRAQMQVRQ LDPATSAYVE TVEFQPGEEG VATPEAYTKV RGEADTRYRV LVAEGTTVWR
VVESLKQADF LSGSVEGEEM PKEGMLAPDS YEVRADSDVD ELIARMQESQ QMRIDTIWAQ
RTEGLPFETP EDMLTLASII EKETGVAEER RQVASVFENR LKRGMRLQTD PTVIYGVTNG
VGVLGRGLRQ SELQSDSPYN TYVVEGLPPG PIANPGFASL EAAVNPDATP YLFFVADGTG
GHAFAETLAE HNANVVKWRE IEAQRASQ
//
