ID A0A1S1R622_9ACTN Unreviewed; 489 AA.
AC A0A1S1R622;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=CC117_13375 {ECO:0000313|EMBL:OHV41181.1};
OS Parafrankia colletiae.
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae;
OC Parafrankia.
OX NCBI_TaxID=573497 {ECO:0000313|EMBL:OHV41181.1, ECO:0000313|Proteomes:UP000179627};
RN [1] {ECO:0000313|Proteomes:UP000179627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cc1.17 {ECO:0000313|Proteomes:UP000179627};
RA Ghodhbane-Gtari F., Swanson E., Gueddou A., Morris K., Hezbri K., Ktari A.,
RA Nouioui I., Abebe-Akele F., Simpson S., Thomas K., Gtari M., Tisa L.S.,
RA Hurst S.;
RT "Sequence Frankia sp. strain CcI1.17.";
RL Submitted (JUL-2016) 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}.
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:OHV41181.1}.
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DR EMBL; MBLM01000058; OHV41181.1; -; Genomic_DNA.
DR RefSeq; WP_071083241.1; NZ_MBLM01000058.1.
DR AlphaFoldDB; A0A1S1R622; -.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000179627; 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:UP000179627};
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 145..164
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT REGION 1..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 366
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 489 AA; 51106 MW; 2D9C2A98AC7D29DE CRC64;
MSRNGGGFDD LFGGAGYDDD RDDRRVGGRA ERHRTAATSG PGRRRQDRAG YADPGYDEAA
YGEAGYGASS HASDDPDSDG YDPAPAGYDP VYADDAGYDG DSAYADDGGY GGGGYGDDGG
AGRRGGRGHP EASGGRRPAR ALPKLIGVLV VVAALLGAGI FGIGKVIGRV GGEPAADYSG
IGEGIVVVQI PAGATSSDIG TALAKADVVA SGRAFVNVAT RDSRALSIQP GTYRLRSKMS
AASALDALLD DASSALFRYT ISPGDTVRRV LQALSARTGT PLAELEALVR DPSSLGLPDY
AGGKLEGYLF PSTYDVAPDT DPVDVLKEAV ARFSAYADEH DIAGRARALG REPGAIVIVA
SIIEKEVANE SEGPKVARVI YNRLADDSGR FRRLDMDSTT RYAANEHEGP LTREQLDNDD
PYNTRAVPGL PPGAIASPSP WALESALNPA DGPWFYFVSM PQTRETVFAA NQAEFDVAMA
EYHRQGGSE
//