ID A0A077F5F1_9PSED Unreviewed; 382 AA.
AC A0A077F5F1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
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=PSAKL28_14960 {ECO:0000313|EMBL:AIL60722.1};
OS Pseudomonas alkylphenolica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=237609 {ECO:0000313|EMBL:AIL60722.1, ECO:0000313|Proteomes:UP000028931};
RN [1] {ECO:0000313|EMBL:AIL60722.1, ECO:0000313|Proteomes:UP000028931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KL28 {ECO:0000313|EMBL:AIL60722.1,
RC ECO:0000313|Proteomes:UP000028931};
RA Lee K., Lim J.Y., Hwang I.;
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 -!- SIMILARITY: Belongs to the transglycosylase MltG family.
CC {ECO:0000256|HAMAP-Rule:MF_02065}.
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DR EMBL; CP009048; AIL60722.1; -; Genomic_DNA.
DR RefSeq; WP_038608602.1; NZ_CP009048.1.
DR AlphaFoldDB; A0A077F5F1; -.
DR KEGG; palk:PSAKL28_14960; -.
DR eggNOG; COG1559; Bacteria.
DR HOGENOM; CLU_025574_0_2_6; -.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000028931; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
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; 3.30.160.60; Classic Zinc Finger; 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 inner membrane {ECO:0000256|HAMAP-Rule:MF_02065};
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 REGION 333..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 218
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 382 AA; 43027 MW; 061103113A5E2724 CRC64;
MRRKFLVLLE TGLILAGLIL GFSAWKVNSA LEQTLHVSQE QLLDVPTGTN PNRMFYRMES
QGLLDDAFWL RLYWRFNMAG VPLHTGEYRM TPGMTVRDLF EVWRRGDVVQ YSLTLVEGWN
FRQVRSALAK HEKIKQTLDG LSDAEVMDEL GHPGVFPEGR FFPDTYRFVR GMTDVEFLQQ
AYARLDEVLA KEWAERPADL PYRDPYQALI MASLVEKETG VPQERGQIAG VFVRRMRIGM
LLQTDPTVIY GMGERYNGKI TRADLREPTP YNTYTNAGLP PTPIAMVGRE AIHAALNPTP
GSSLYFVARG DGSHIFSDDL DAHNSAVREY QIKRRADYRS SPAPVTESEP EPEAGPQSSE
PTEAIPEPLP EASAPATETS SQ
//
