ID A0A154QX55_9GAMM Unreviewed; 344 AA.
AC A0A154QX55;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=RhoFW510R10_05280 {ECO:0000313|EMBL:KZC29586.1};
OS Rhodanobacter sp. FW510-R10.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=1524462 {ECO:0000313|EMBL:KZC29586.1, ECO:0000313|Proteomes:UP000076310};
RN [1] {ECO:0000313|EMBL:KZC29586.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FW510-R10 {ECO:0000313|EMBL:KZC29586.1};
RX PubMed=27048805; DOI=10.1128/mBio.02234-15;
RA Hemme C.L., Green S.J., Rishishwar L., Prakash O., Pettenato A.,
RA Chakraborty R., Deutschbauer A.M., Van Nostrand J.D., Wu L., He Z.,
RA Jordan I.K., Hazen T.C., Arkin A.P., Kostka J.E., Zhou J.;
RT "Lateral Gene Transfer in a Heavy Metal-Contaminated-Groundwater Microbial
RT Community.";
RL MBio 7:e02234-e02215(2016).
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}.
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:KZC29586.1}.
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DR EMBL; LVJU01000117; KZC29586.1; -; Genomic_DNA.
DR RefSeq; WP_068091074.1; NZ_LVJU01000117.1.
DR AlphaFoldDB; A0A154QX55; -.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000076310; 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 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 SITE 226
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 344 AA; 37699 MW; 9B16BA6B39C29F61 CRC64;
MSDKPTRKRA WPRLLLIVLL VAAGALAYGW NDYARFGTTP LNVTARGESI DVGRGSSFKA
IVGELRQRGF STANSWYWRL LARQTHVAGR LHAGEYALEP GITPRQLLAN MAAGKVLQRN
VTIVDGWTFG ELRQALARAE KLNHDSAGLD DAAIMQKIGA GGETPEGRFL PETYAYVKGD
GDLDILRRAH AAMVKTLDEL WAGRAQGLPL ASPYEALILA SIVEKETGRP DERAQIAGVF
VRRLRNHMLL QTDPSVIYGM GASYAGNIHK SDLTTDTPYN TYTRAGLPPT PIALPGKPAL
VAALHPADGD TLYFVARGDG GHVFSRTLEE HNRNVDCYQR KRCR
//
