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Database: UniProt
Entry: A0A1E7JUA0_9ACTN
LinkDB: A0A1E7JUA0_9ACTN
Original site: A0A1E7JUA0_9ACTN 
ID   A0A1E7JUA0_9ACTN        Unreviewed;       561 AA.
AC   A0A1E7JUA0;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
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=AN215_01595 {ECO:0000313|EMBL:OEU93520.1};
OS   Streptomyces abyssalis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=933944 {ECO:0000313|EMBL:OEU93520.1, ECO:0000313|Proteomes:UP000176087};
RN   [1] {ECO:0000313|EMBL:OEU93520.1, ECO:0000313|Proteomes:UP000176087}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCSIO 10390 {ECO:0000313|EMBL:OEU93520.1,
RC   ECO:0000313|Proteomes:UP000176087};
RX   PubMed=27446038; DOI=10.3389/fmicb.2016.00998;
RA   Tian X., Zhang Z., Yang T., Chen M., Li J., Chen F., Yang J., Li W.,
RA   Zhang B., Zhang Z., Wu J., Zhang C., Long L., Xiao J.;
RT   "Comparative Genomics Analysis of Streptomyces Species Reveals Their
RT   Adaptation to the Marine Environment and Their Diversity at the Genomic
RT   Level.";
RL   Front. Microbiol. 7:998-998(2016).
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}.
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:OEU93520.1}.
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DR   EMBL; LJGT01000036; OEU93520.1; -; Genomic_DNA.
DR   RefSeq; WP_070012628.1; NZ_LJGT01000036.1.
DR   AlphaFoldDB; A0A1E7JUA0; -.
DR   STRING; 933944.AN215_01595; -.
DR   PATRIC; fig|933944.5.peg.2586; -.
DR   OrthoDB; 9814591at2; -.
DR   Proteomes; UP000176087; Unassembled WGS sequence.
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; 3.30.1490.480; 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:UP000176087};
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        214..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT   REGION          1..213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          538..561
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        46..71
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        176..203
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            438
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ   SEQUENCE   561 AA;  59752 MW;  12C2A2481C7569AE CRC64;
     MTEYGRGQSL PPWHPDDPLF GDTWDGGRDT SYPGDGDPHA GQYADPYSTG QHQVPHQQGY
     YGQQPQQQYY GQGGYDGGGA GSPYDAGHGA GATNPHGMPV VNDPYDTGAQ PGYYAAQQGH
     PQQQPHGQGY PGPYGQPGAD GYLAPHPGGP GGPGGPGGRP DADPETGWDP GPDQGEHAFF
     ADRDDGDGDF DHEDGDGRSK RSGRRGGEPK KRRGGCACLA VSLVLAGGLG TAGYFGYDFY
     KTYFAPAPDY SGKGSGQAQV KIPDGASIAD MGNELQQAGV VKSAGAFVEA AQAEKKSSGI
     QPGTYSLRKQ MSGAAAVKLM LDPASQNGLI ISEGRRAKAV YELVDDKLGK PKGTTEKAAK
     NARASDLGLP RFAKGNPEGF LFPSRYSVGE ESDPLDVLRD MIARAKAEHT KVDLAGEAKK
     VGKSPEEILT IASLIQAEAQ QDEEFGRVSR VIYNRLDKDI LLQFDSTINY AKGRSSLETS
     VEDTRFKSPY NTYLNRGLPP GPIDNPGHQA IEAALNPTKG NWIYFVTVKP GDTRFTASKA
     EHDRNVQDFN KEQRKKKGNG G
//
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