ID A0A7J5AQ18_9FLAO Unreviewed; 342 AA.
AC A0A7J5AQ18;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 02-APR-2025, entry version 10.
DE RecName: Full=Endolytic murein transglycosylase {ECO:0000256|HAMAP-Rule:MF_02065};
DE EC=4.2.2.29 {ECO:0000256|HAMAP-Rule:MF_02065};
DE AltName: Full=Peptidoglycan lytic transglycosylase {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 ECO:0000313|EMBL:KAB1159680.1};
GN ORFNames=F7018_05050 {ECO:0000313|EMBL:KAB1159680.1};
OS Tenacibaculum aiptasiae.
OC Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Tenacibaculum.
OX NCBI_TaxID=426481 {ECO:0000313|EMBL:KAB1159680.1, ECO:0000313|Proteomes:UP000467305};
RN [1] {ECO:0000313|EMBL:KAB1159680.1, ECO:0000313|Proteomes:UP000467305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=a4 {ECO:0000313|Proteomes:UP000467305};
RA Cao W.R.;
RL Submitted (SEP-2019) 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 -!- CATALYTIC ACTIVITY:
CC Reaction=a peptidoglycan chain = a peptidoglycan chain with N-
CC acetyl-1,6-anhydromuramyl-[peptide] at the reducing end + a
CC peptidoglycan chain with N-acetylglucosamine at the non-reducing
CC end.; EC=4.2.2.29; Evidence={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:KAB1159680.1}.
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DR EMBL; WAAU01000008; KAB1159680.1; -; Genomic_DNA.
DR RefSeq; WP_150898927.1; NZ_WAAU01000008.1.
DR AlphaFoldDB; A0A7J5AQ18; -.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000467305; 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; 3.30.160.60; Classic Zinc Finger; 1.
DR HAMAP; MF_02065; MltG; 1.
DR InterPro; IPR003770; MLTG-like.
DR NCBIfam; TIGR00247; endolytic transglycosylase MltG; 1.
DR PANTHER; PTHR30518; ENDOLYTIC MUREIN TRANSGLYCOSYLASE; 1.
DR PANTHER; PTHR30518:SF2; ENDOLYTIC MUREIN TRANSGLYCOSYLASE; 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:UP000467305};
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 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT SITE 212
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 342 AA; 39391 MW; E8BEF45BC2695936 CRC64;
MNKKIIYGVI AILFVVGGII GFNFYQKIFG NAVKKDGAIY IGSNYHLIDV KKLLTEYINK
PENFIWVAEK KKFTKPKGGK YILKKGMSMN DVVNLLRSGN QTPVKVSFNN QDTLEKLAGR
IAQQIETDSI SLLQAMIDET FLAKNGFNKQ TALEIYIPNS YQFYWNTSAN KFRDKMLREY
KRFWNQSRLD KAKKLNLTKS EVIALASIVQ KETAQKSERP IVAGLYLNRL KDNWPLQADP
TLIYAIKQLK GQDFVVKRVL NKDKEIKSPY NTYMHTGLPP SLIAMPDVSS IDAVLNYKKH
NYYYMCASTE KIGFHDFAKS LAQHNRNAAK YQKWISQRGI RR
//
