ID A0A0C1QIL2_9RICK Unreviewed; 329 AA.
AC A0A0C1QIL2;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=NF27_DT01230 {ECO:0000313|EMBL:KIE05349.1};
OS Candidatus Jidaibacter acanthamoeba.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Candidatus Midichloriaceae; Jidaibacter.
OX NCBI_TaxID=86105 {ECO:0000313|EMBL:KIE05349.1, ECO:0000313|Proteomes:UP000031258};
RN [1] {ECO:0000313|EMBL:KIE05349.1, ECO:0000313|Proteomes:UP000031258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UWC36 {ECO:0000313|EMBL:KIE05349.1,
RC ECO:0000313|Proteomes:UP000031258};
RA Schulz F., Martijn J., Wascher F., Kostanjsek R., Ettema T.J., Horn M.;
RT "A Rickettsiales Symbiont of Amoebae With Ancient Features.";
RL Submitted (NOV-2014) 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 inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_02065}; Single-pass membrane protein {ECO:0000256|HAMAP-
CC 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:KIE05349.1}.
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DR EMBL; JSWE01000096; KIE05349.1; -; Genomic_DNA.
DR RefSeq; WP_039456430.1; NZ_JSWE01000096.1.
DR AlphaFoldDB; A0A0C1QIL2; -.
DR STRING; 86105.NF27_DT01230; -.
DR PATRIC; fig|86105.3.peg.923; -.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000031258; 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 inner membrane {ECO:0000256|HAMAP-Rule:MF_02065};
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 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 9..28
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT SITE 205
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 329 AA; 37304 MW; 11EF4C48AFE8EB21 CRC64;
MHSKLKKFFI IYLIFKLLLI TAVVYSYHNT FYKTHVHQEK IVIIPKNYSI NQIADLLHKK
DVIKSKLLFI LLSKAHSFKK EYLQSGEYKF EAGMKMIEVI HKLTRGEVII HKVTIPEGLT
NSQVFKILDN SYGLSGSINK EKYKEGYLLP ETYSYKYGTK KESVLARMHS SMEKHLTLFI
STSALPIPLK DVNELLTLAS IVEKESGINA EKPLVAGVYL NRLKINMPLQ ADPTVIYGMT
GGVEPFPKRL TYKDLESASL YNTYKVKGLP PTPIANPGLR SIAAVLHPAN TKDLFFVADG
LGGHKFSETY KKHLTNVKNF RTFTGKKSE
//