ID I8AIH8_9BACI Unreviewed; 391 AA.
AC I8AIH8;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 39.
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=A374_11090 {ECO:0000313|EMBL:EIT85284.1};
OS Fictibacillus macauensis ZFHKF-1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Fictibacillus.
OX NCBI_TaxID=1196324 {ECO:0000313|EMBL:EIT85284.1, ECO:0000313|Proteomes:UP000004080};
RN [1] {ECO:0000313|EMBL:EIT85284.1, ECO:0000313|Proteomes:UP000004080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZFHKF-1 {ECO:0000313|EMBL:EIT85284.1,
RC ECO:0000313|Proteomes:UP000004080};
RX PubMed=22887677; DOI=10.1128/JB.01049-12;
RA Cai L., Zhang T.;
RT "Genome of Bacillus macauensis ZFHKF-1, a Long-Chain-Forming Bacterium.";
RL J. Bacteriol. 194:4780-4780(2012).
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:EIT85284.1}.
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DR EMBL; AKKV01000026; EIT85284.1; -; Genomic_DNA.
DR RefSeq; WP_007202302.1; NZ_AKKV01000026.1.
DR AlphaFoldDB; I8AIH8; -.
DR STRING; 1196324.A374_11090; -.
DR PATRIC; fig|1196324.3.peg.2274; -.
DR eggNOG; COG1559; Bacteria.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000004080; 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:UP000004080};
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 42..61
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT SITE 269
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 391 AA; 44257 MW; 1EC56456EB79F5C9 CRC64;
MNFTYQYNKA DERGDKLMLL LNTVSGGPLP NGPKKKRTGL KIALSLFVVL LAVLIFGYTY
IKSALGPLNS EKEQDITVMI SQGSSINDIG DQLEKKGVIK SSTIFAWYAK YKNESNLKAG
TYDFTTGMDA DQILSVLTEG KEGMRHHVSI TIPEGFTVPK VAKVIAKQTG QSEESVLQVM
NDRAFVKELQ GKYPIIDKKV FNKKIYYPLE GYLFPAKYVF NTKKTSVKEI VTRMVAKTEN
VLDLYKKDMK DMKKTPYQLL TMAAIVEGEA QADQDRGKIA GVFYNRIKKQ IPLGSDPTVK
YARKNFKVKL LYKELKIDSP YNTYKYKGLP IGPINSPGEP SIKAALHPEK SDYLFFYARP
SGEVIYTKNF ADHQKAINRY KSEWKKHEEQ G
//
