ID A0A098Y5D4_9ACTN Unreviewed; 682 AA.
AC A0A098Y5D4;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=IN07_20775 {ECO:0000313|EMBL:KGH44891.1};
OS Modestobacter caceresii.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Modestobacter.
OX NCBI_TaxID=1522368 {ECO:0000313|EMBL:KGH44891.1, ECO:0000313|Proteomes:UP000029713};
RN [1] {ECO:0000313|EMBL:KGH44891.1, ECO:0000313|Proteomes:UP000029713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KNN45-2b {ECO:0000313|EMBL:KGH44891.1,
RC ECO:0000313|Proteomes:UP000029713};
RA Bukarasam K., Bull A., Girard G., van Wezel G., Goodfellow M.;
RT "Biosystematic studies on Modestobacter strains isolated from extreme
RT hyper-arid desert soil and from historic building.";
RL Submitted (JUL-2014) 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:KGH44891.1}.
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DR EMBL; JPMX01000107; KGH44891.1; -; Genomic_DNA.
DR RefSeq; WP_036339543.1; NZ_JPMX01000107.1.
DR AlphaFoldDB; A0A098Y5D4; -.
DR STRING; 1522368.IN07_20775; -.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000029713; 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:UP000029713};
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 343..367
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 36..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 559
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 682 AA; 70161 MW; D0DF6691676F7B14 CRC64;
MTDPTQPHAS GRHSDADAGA GRPAAEFLAA WAGAATLQLP DDPADATLRP RRRRRHAPDT
GARVGPAGGG VDVADVEITG LAASGIADAG LAAAGLDVSA FDLGRRSATP VAPRGPGGIA
PGARAREVTV PQTAEMPAVP PAVPTIGGAA HGAGPAAARR LPAPRPSTEP TTADHVRADR
FADAGTDPGW LSAANRPVPG PVGPSSVPTS GPSGALAGLV TGQGGTEVRT APRDTPVDEP
ATVVHAALTV DGADPDEERW RMVSERHGSD EGDLDPAHHD PHDDGAFASA SPQTGGLDVI
GGGDHDEHHD EYYDGHDDGH DDGGVGGGGR RGAGGRGGRR GPVVVVLSLV VLAALVAGIF
IGGKALWNRV NPVAEDYPGA GTGEVDVRVE PGDSLRAIGT TLVEADVIAS VAPFTEAAEA
NPAATGIQPG VYRLRQQMSG QAALDLLLDP ASRQVTRVTL PEGLRVTQVL QRLADESGLP
LAELEAAAAD PAQLGLPAYA NGLLEGFLFP ATYDIEPGET AVEVLSEMVA RTDQVLTELQ
IPVEQRLTAL TKASLVQAEA GSIEDMGKVA RVLENRLADG MPLQLDTTVN YANDKAGITT
SAEDRANPSL YNTYVHPGLP PGAINNPGEE ALRAVLDPTP GDWRFFVVVD PDTGETRFAA
TGAEHQQNVL LFQQWLRDNP GN
//
