ID A0A239SWH0_9STRE Unreviewed; 555 AA.
AC A0A239SWH0;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=pabC {ECO:0000313|EMBL:SNU89084.1};
GN Synonyms=mltG {ECO:0000256|HAMAP-Rule:MF_02065};
GN ORFNames=SAMEA4412692_01342 {ECO:0000313|EMBL:SNU89084.1};
OS Streptococcus merionis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=400065 {ECO:0000313|EMBL:SNU89084.1, ECO:0000313|Proteomes:UP000215185};
RN [1] {ECO:0000313|EMBL:SNU89084.1, ECO:0000313|Proteomes:UP000215185}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13788 {ECO:0000313|EMBL:SNU89084.1,
RC ECO:0000313|Proteomes:UP000215185};
RG Pathogen Informatics;
RL Submitted (JUN-2017) 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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_02065};
CC Single-pass membrane protein {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; LT906439; SNU89084.1; -; Genomic_DNA.
DR RefSeq; WP_018373275.1; NZ_LT906439.1.
DR AlphaFoldDB; A0A239SWH0; -.
DR STRING; 1123308.GCA_000380085_00706; -.
DR KEGG; smen:SAMEA4412692_1342; -.
DR eggNOG; COG1559; Bacteria.
DR Proteomes; UP000215185; Chromosome 1.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 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:UP000215185};
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 TRANSMEM 184..207
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT REGION 130..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 427
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 555 AA; 61239 MW; E03E2E7E0E240135 CRC64;
MSDKLNPNDQ ELTFKERILR DLEILKSQVE EADETAFNQV KSDEETQGVA VAEIERLKAD
LESKLSGPSE EGQPVKAEEV PDFVAEQARK LSEQSLEPPL RQSVIPEPEA VPYKVDLTFN
PEVDPNEEFM ETEKAEASSV APVDASSQSG NEMAPTRRSR SAYPDRAPKK NKKVKKKKSK
ARKLTVWIFT TLLLVLVATS VAGYFFVKDS LGPVDAKSTE YVQVQIAEGS SVKAIAQTLE
KEGVIKNATV FDLYAKVKNL SGFQSGYHQL QKSMNVDEII AVLQQEGTAE EVVPAKGKVT
IPEGYTLKQI SEAVAVNAAS STKASSPFTA EEFMSLVTDE TFIAEMQAKY PDLLGGLPTA
DTGVIYRLEG YLFPATYEYQ EGTTIRDLVD QMLGAMDANL RPYYETISAK EQTVNQILTL
ASLVEKEGSS DQDRKNIASV FYNRMQFGMP LQSNIAILYA EGKLGEKITL AEDATINTQI
ESPYNVYTHL GYMPGPVDSP SLSAIKATIE PSTTEYFYFV ADVTTGQVYF ANTIEEHNTN
VQTYVNEKIQ SSTGQ
//
