ID A0A1K2FLS3_9ACTN Unreviewed; 562 AA.
AC A0A1K2FLS3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=STEPF1_01184 {ECO:0000313|EMBL:SFY47967.1};
OS Streptomyces sp. F-1.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=463642 {ECO:0000313|EMBL:SFY47967.1, ECO:0000313|Proteomes:UP000095403};
RN [1] {ECO:0000313|EMBL:SFY47967.1, ECO:0000313|Proteomes:UP000095403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Streptomyces sp. F1 {ECO:0000313|EMBL:SFY47967.1};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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}.
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DR EMBL; FKJI03000002; SFY47967.1; -; Genomic_DNA.
DR RefSeq; WP_071828518.1; NZ_FKJI03000002.1.
DR AlphaFoldDB; A0A1K2FLS3; -.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000095403; 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 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:UP000095403};
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 207..230
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT REGION 1..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 438
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 562 AA; 61280 MW; 2D7702CF4414F921 CRC64;
MTEYGRGPGS EPWHPQDPLY GDGGWEGQQA YAGHQAAYGG RSQQQYPQQP QHGDWQQMPQ
PGYDGQQYPY YADQGQTPYD PQYPGQHPQP GQHPQPGHQG GWDATGTHGQ VPYAADPGDP
YGQQPVAYGA EQPDFYAAED AYPPPEPPGR RRPEAEPEPD PAVDGEEEHA FFAGGDDEDD
EPHERAGRAE RRAGKGRKPV KSKKRRTGCA CMVVVLVFGG GLGGVGYYGY KFYQNRFAPA
PDYAGDGTGE TVTVEIPKGA GGWDIGRRLK EAGVVKSAEA FVHAQGTTPG GDSIQAGAYL
LKKEMSAASA VRMMLDPKSQ NNVMVRPGER NAGVYQDIDK KLQLAAGTTQ KIAAKEYRTF
GLPSWVSSDS NIKDPLEGFL FPGSYAAAKG MKPDAILKQM VAQAKERYAA YGLDAKARSL
GLHNAFELVT VASLVQAEGK THDDFRKMAE VVYNRLKPTN TETNQLLQFD STYNYLKGTS
NIHISEKDIN SNQSPYNTYT HKGLPPGPIG NPGEDALKAT LNPTHDGWIY FVATDGTTNT
EFAKTYEEFK QLKDKFNATS GN
//
