ID A0A1Q8Z8B2_9CYAN Unreviewed; 368 AA.
AC A0A1Q8Z8B2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
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=BST81_21610 {ECO:0000313|EMBL:OLP16387.1};
OS Leptolyngbya sp. 'hensonii'.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC Leptolyngbya group; Leptolyngbya.
OX NCBI_TaxID=1922337 {ECO:0000313|EMBL:OLP16387.1, ECO:0000313|Proteomes:UP000186296};
RN [1] {ECO:0000313|EMBL:OLP16387.1, ECO:0000313|Proteomes:UP000186296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=hensonii {ECO:0000313|Proteomes:UP000186296};
RA Hamilton T.L., Klatt J.M., De Beer D., Macalady J.;
RT "Physiology of photosynthesis in the novel isolate Oscillatoriales
RT cyanobacterium hensonii.";
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}.
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:OLP16387.1}.
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DR EMBL; MQTZ01000050; OLP16387.1; -; Genomic_DNA.
DR RefSeq; WP_075600585.1; NZ_MQTZ01000050.1.
DR AlphaFoldDB; A0A1Q8Z8B2; -.
DR STRING; 1922337.BST81_21610; -.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000186296; 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 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:UP000186296};
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 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT SITE 236
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 368 AA; 41161 MW; 93FF8ABA07B1B713 CRC64;
MKTVQRTPKW SLYVVPVLLG VCIWQGWAWW SWATMPPIVP GQVSLVPGEK PIRIQISPGT
PSQHIGQDLK SAGLIRSAQA WNLWARWLSL RDQQGGFQAG TYELSPTQSM QTIAAKIWAG
ETVQFSFTIP EGWSLRQMAA YFESQGFFKA QDFLTTAQQI PSDQFAWLPS GIPHVEGFLY
PDTYQLASDR ITPSEVIRKM LVRFEQLALP VYQQQRQKPS LTLLEWVTLA SIVEKEAVIP
TERPQIAGVF VNRLKLKMPL GADPTVEYGL NVQQTPDQPL TLAQVRTPSA YNTYLNVGLP
PTPIASPGLA SLEASLYPEN TPYLYFVARY DGTHVFSRTL QEHEAAQAAI RDAQSTRQKA
NPATKPLP
//
