ID J1YZ11_9NOCA Unreviewed; 579 AA.
AC J1YZ11;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=JVH1_8936 {ECO:0000313|EMBL:EJI93640.1};
OS Rhodococcus sp. JVH1.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=745408 {ECO:0000313|EMBL:EJI93640.1, ECO:0000313|Proteomes:UP000009024};
RN [1] {ECO:0000313|EMBL:EJI93640.1, ECO:0000313|Proteomes:UP000009024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JVH1 {ECO:0000313|EMBL:EJI93640.1,
RC ECO:0000313|Proteomes:UP000009024};
RX PubMed=22965106; DOI=10.1128/JB.01066-12;
RA Brooks S.L., Van Hamme J.D.;
RT "Whole-Genome Shotgun Sequence of Rhodococcus Species Strain JVH1.";
RL J. Bacteriol. 194:5492-5493(2012).
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:EJI93640.1}.
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DR EMBL; AKKP01000126; EJI93640.1; -; Genomic_DNA.
DR RefSeq; WP_009480410.1; NZ_AKKP01000126.1.
DR AlphaFoldDB; J1YZ11; -.
DR PATRIC; fig|745408.3.peg.8476; -.
DR Proteomes; UP000009024; 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 Gene3D; 3.30.1490.480; Endolytic murein transglycosylase; 1.
DR HAMAP; MF_02065; MltG; 1.
DR InterPro; IPR003770; MLTG-like.
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 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 205..226
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 458
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 579 AA; 62909 MW; E80577AD33251E7C CRC64;
MSNHRRPAGE RPEFQYVPRE PRRHRYLDED DDQVDYAPPP EDDDVVTTGR HAVVYDDRDV
DEPPAHYTEP VYEQPVYEDP VYEDPVYERP VYEQPFDPEP VYEDGYGPRS YGDARAYREP
AADDHAYDEP AYVEEPAYVD EQYGSYTHPD DRYDTPPDQP DVAFAEAETQ IISAIPEEIP
PTRAHARTQA RRRKQATGRA RRGKLFGVLA AATVLTVLIG VVFVGGKMFF GGPDAPADYA
GPGGPDVVVQ VHPGDTAEEI ASTLAERDVV ASGSAFFNAA VQSNAMNSVQ PGFYSLSTQI
PADDAVQELI DPTSRVGQMI ISEGRQLHDT TDVQTGAKKK GIYTLISEAS CIGEAGQEQC
IGYDDLNAAG AGDLSALGVP DWAKDAVAGV PDRDRQLEGL IAAGSWDFDP TAGPAAILQR
LVTESSASYE KTGILTAGNQ VGLTPYKMLI AASLVEREAM PDDFSKVARV ILNRLAVNQA
LQFDSTVNYA LDTTELATTD ADRAQVTPWN TYASPGLPAT PISSPSIGAL QAVEQPAPGD
WIYFVTVDSK GTTLFTKSYD EHLANIDQAL NNGILNSGR
//
