ID A0A1M7M2Z3_9FIRM Unreviewed; 449 AA.
AC A0A1M7M2Z3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=SAMN02746066_03554 {ECO:0000313|EMBL:SHM84559.1};
OS Anaerosporobacter mobilis DSM 15930.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Anaerosporobacter.
OX NCBI_TaxID=1120996 {ECO:0000313|EMBL:SHM84559.1, ECO:0000313|Proteomes:UP000184038};
RN [1] {ECO:0000313|EMBL:SHM84559.1, ECO:0000313|Proteomes:UP000184038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15930 {ECO:0000313|EMBL:SHM84559.1,
RC ECO:0000313|Proteomes:UP000184038};
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 -!- SIMILARITY: Belongs to the transglycosylase MltG family.
CC {ECO:0000256|HAMAP-Rule:MF_02065}.
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DR EMBL; FRCP01000019; SHM84559.1; -; Genomic_DNA.
DR RefSeq; WP_073289750.1; NZ_FRCP01000019.1.
DR AlphaFoldDB; A0A1M7M2Z3; -.
DR STRING; 1120996.SAMN02746066_03554; -.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000184038; Unassembled WGS sequence.
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 HAMAP; MF_02065; MltG; 1.
DR InterPro; IPR012854; Cu_amine_oxidase-like_N.
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; PF07833; Cu_amine_oxidN1; 1.
DR Pfam; PF02618; YceG; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000184038};
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 DOMAIN 69..159
FT /note="Copper amine oxidase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF07833"
FT SITE 331
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 449 AA; 50734 MW; 7BC0702FAFAE41D2 CRC64;
MKNSKYARLT ISILMIVIIL SCNLLNRSLT NVEASSAGKY GVLIADAKGK YTFFDWNSEQ
GTQRIIKKSS NIMLPLRRTC SNLTNIEYSY DFTTNKATVT NTKNGKKIIF TKDSKTAYTY
ASKKAKAKKV TLKYKMYLDK DSNAAMVEAS ALSYVLSAKS GYKLYSSDTA LKDAGYSVKQ
YAGVIVLNPY KKVSTLPAAT KVKYISEKIA SNVKKVTIPE GYSVAQVFEL LVEKGVCASV
DALFAASEEI DYSASKSISS QLLKENRCFT LEGYLYPDTY EFYGNSEPSD VLKKIVANTD
KKYTEEYYTR AEELGYTLDE IITIASIIEK ETGKDAERAK IGSVLYNRLE IGMRLQCDCT
IYYIERYVKP YITGDINRYN DYYNTRKCKA LPDGPIANPG KKAIQAALYP AETEYYYFCS
DKEGEYHYFK TYEEQKDFLN SIETSDSKQ
//
