ID   MLTG_STRR6              Reviewed;         551 AA.
AC   Q8CYJ8;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Endolytic murein transglycosylase {ECO:0000255|HAMAP-Rule:MF_02065};
DE            EC=4.2.2.- {ECO:0000255|HAMAP-Rule:MF_02065};
DE   AltName: Full=Peptidoglycan polymerization terminase {ECO:0000255|HAMAP-Rule:MF_02065};
GN   Name=mltG {ECO:0000255|HAMAP-Rule:MF_02065}; OrderedLocusNames=spr1370;
OS   Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=171101;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-255 / R6;
RX   PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA   Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA   DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA   Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA   Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA   McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA   Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA   Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA   Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT   "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL   J. Bacteriol. 183:5709-5717(2001).
RN   [2]
RP   FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ALA-505.
RC   STRAIN=R6 / R704;
RX   PubMed=28710862; DOI=10.1111/mmi.13748;
RA   Stamsaas G.A., Straume D., Ruud Winther A., Kjos M., Frantzen C.A.,
RA   Haavarstein L.S.;
RT   "Identification of EloR (Spr1851) as a regulator of cell elongation in
RT   Streptococcus pneumoniae.";
RL   Mol. Microbiol. 105:954-967(2017).
RN   [3]
RP   INTERACTION WITH KHPB, AND PROBABLE TOPOLOGY.
RC   STRAIN=R6 / R704;
RX   PubMed=33558392; DOI=10.1128/jb.00691-20;
RA   Winther A.R., Kjos M., Herigstad M.L., Haavarstein L.S., Straume D.;
RT   "EloR interacts with the lytic transglycosylase MltG at midcell in
RT   Streptococcus pneumoniae R6.";
RL   J. Bacteriol. 0:0-0(2021).
CC   -!- FUNCTION: Functions as a peptidoglycan terminase that cleaves nascent
CC       peptidoglycan strands endolytically to terminate their elongation.
CC       {ECO:0000255|HAMAP-Rule:MF_02065}.
CC   -!- FUNCTION: Mutations in this gene suppress deletion of PBP2b (penA);
CC       truncation at residue 168, undefined changes between residue Ile-447
CC       and Ala-505, and mutation of Ala-505 suppress the penA deletion.
CC       Probably part of the elongasome which synthesizes peripheral
CC       peptidogylcan. {ECO:0000269|PubMed:28710862}.
CC   -!- SUBUNIT: Interacts with RodZ. Interacts with MreC in the elongasome;
CC       interaction is strongly reduced when the 90 C-terminal residues of MreC
CC       are missing (PubMed:28710862). Interacts with KhpB (also called
CC       EloR/Jag) via MltG's N-terminus, suggesting the N-terminus of MltG is
CC       cytoplasmic (PubMed:33558392). {ECO:0000269|PubMed:28710862,
CC       ECO:0000269|PubMed:33558392}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_02065,
CC       ECO:0000269|PubMed:28710862}; Single-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_02065}. Note=Localizes to midcell in the
CC       presence and absence of khpB (also called eloR/jag).
CC       {ECO:0000269|PubMed:28710862}.
CC   -!- DEVELOPMENTAL STAGE: Essential, it cannot be deleted.
CC       {ECO:0000269|PubMed:33558392}.
CC   -!- SIMILARITY: Belongs to the transglycosylase MltG family.
CC       {ECO:0000255|HAMAP-Rule:MF_02065}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE007317; AAL00174.1; -; Genomic_DNA.
DR   PIR; A98043; A98043.
DR   RefSeq; NP_358963.1; NC_003098.1.
DR   RefSeq; WP_001291640.1; NC_003098.1.
DR   AlphaFoldDB; Q8CYJ8; -.
DR   SMR; Q8CYJ8; -.
DR   STRING; 171101.spr1370; -.
DR   EnsemblBacteria; AAL00174; AAL00174; spr1370.
DR   GeneID; 60233120; -.
DR   KEGG; spr:spr1370; -.
DR   PATRIC; fig|171101.6.peg.1485; -.
DR   eggNOG; COG1559; Bacteria.
DR   HOGENOM; CLU_025574_1_0_9; -.
DR   OMA; IAMPGKA; -.
DR   Proteomes; UP000000586; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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   HAMAP; MF_02065; MltG; 1.
DR   InterPro; IPR003770; MLTG-like.
DR   PANTHER; PTHR30518; PTHR30518; 1.
DR   Pfam; PF02618; YceG; 1.
DR   TIGRFAMs; TIGR00247; TIGR00247; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Cell wall biogenesis/degradation; Lyase; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..551
FT                   /note="Endolytic murein transglycosylase"
FT                   /id="PRO_0000454549"
FT   TOPO_DOM        1..187
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:33558392"
FT   TRANSMEM        188..208
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02065"
FT   TOPO_DOM        209..551
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305|PubMed:33558392"
FT   REGION          38..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..104
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        160..178
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            428
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02065"
FT   MUTAGEN         505
FT                   /note="A->V: Suppresses a PBP2b (penA) deletion."
FT                   /evidence="ECO:0000269|PubMed:28710862"
SQ   SEQUENCE   551 AA;  60813 MW;  B99F25A50DF0206A CRC64;
     MSEKSREEEK LSFKEQILRD LEKVKGYDEV LKEDEAVVRT PANEPSAEEL MADSLSTVEE
     IMRKAPTVPT HPSQGVPASP ADEIQRETPG VPSHPSQDVP SSPAEESGSR PGPGPVRPKK
     LEREYNETPT RVAVSYTTAE KKAEQAGPET PTPATETVDI IRDTSRRSRR EGAKPAKPKK
     EKKSHVKAFV ISFLVFLALL SAGGYFGYQY VLDSLLPIDA NSKKYVTVGI PEGSNVQEIG
     TTLEKAGLVK HGLIFSFYAK YKNYTDLKAG YYNLQKSMST EDLLKELQKG GTDEPQEPVL
     ATLTIPEGYT LDQIAQTVGQ LQGDFKESLT AEAFLAKVQD ETFISQAVAK YPTLLESLPV
     KDSGARYRLE GYLFPATYSI KESTTIESLI DEMLAAMDKN LSLYYSTIKS KNLTVNELLT
     IASLVEKEGA KTEDRKLIAG VFYNRLNRDM PLQSNIAILY AQGKLGQNIS LAEDVAIDTN
     IDSPYNVYKN VGLMPGPVDS PSLDAIESSI NQTKSDNLYF VADVTEGKVY YANNQEDHDR
     NVAEHVNSKL N