ID H3ZJ33_9ALTE Unreviewed; 349 AA.
AC H3ZJ33;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=AJE_17004 {ECO:0000313|EMBL:EHR39502.1};
OS Alishewanella jeotgali KCTC 22429.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Alishewanella.
OX NCBI_TaxID=1129374 {ECO:0000313|EMBL:EHR39502.1, ECO:0000313|Proteomes:UP000012046};
RN [1] {ECO:0000313|EMBL:EHR39502.1, ECO:0000313|Proteomes:UP000012046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 22429 {ECO:0000313|EMBL:EHR39502.1,
RC ECO:0000313|Proteomes:UP000012046};
RX PubMed=22461542; DOI=10.1128/JB.00153-12;
RA Jung J., Chun J., Park W.;
RT "Genome Sequence of Extracellular-Protease-Producing Alishewanella jeotgali
RT Isolated from Traditional Korean Fermented Seafood.";
RL J. Bacteriol. 194:2097-2097(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:EHR39502.1}.
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DR EMBL; AHTH01000055; EHR39502.1; -; Genomic_DNA.
DR RefSeq; WP_008951897.1; NZ_AHTH01000055.1.
DR AlphaFoldDB; H3ZJ33; -.
DR STRING; 1129374.AJE_17004; -.
DR PATRIC; fig|1129374.4.peg.3371; -.
DR eggNOG; COG1559; Bacteria.
DR Proteomes; UP000012046; 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 230
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 349 AA; 39963 MW; 9B4E0BFA758BAB29 CRC64;
MLRRLSYWLP VLLVLVLVAG NSYWQQAQQA LLAAPIRFSE ALYEVKPGAS ARQLCRQWQT
QQQLTAWQCQ QLKLYLRQHP EQAQLQQGLY RVEAEMSLQQ ALALFRSGRV AQFSVTLIEG
ETLAQSWQRF ADLPYLQQDL QQIAELQQLL RWPAEWGELA PMPELAQQME GLFFPDTYFY
TANSKASAIW LRAHQALLTQ LEQIWQQRQP DLPLQTPYQL LILASIIEKE SGLQAERGLV
SSVFVNRLNT GMRLQTDPTV IYGVADYNGR ITRAHLRDPH PYNTYRHHGL PPGPISLVSI
SALKAAAAPE QSDYYYFVSR GDGSHVFSQT LEQHNSAVRK YILGQNNEQ
//
