ID N6URG6_BARVB Unreviewed; 369 AA.
AC N6URG6;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 13-SEP-2023, entry version 28.
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=BVtw_06290 {ECO:0000313|EMBL:ENN94939.1};
OS Bartonella vinsonii subsp. berkhoffii str. Tweed.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=1094502 {ECO:0000313|EMBL:ENN94939.1, ECO:0000313|Proteomes:UP000014011};
RN [1] {ECO:0000313|EMBL:ENN94939.1, ECO:0000313|Proteomes:UP000014011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tweed {ECO:0000313|EMBL:ENN94939.1};
RX PubMed=23555299; DOI=10.1371/journal.pgen.1003393;
RA Guy L., Nystedt B., Toft C., Zaremba-Niedzwiedzka K., Berglund E.C.,
RA Granberg F., Naslund K., Eriksson A.S., Andersson S.G.;
RT "A gene transfer agent and a dynamic repertoire of secretion systems hold
RT the keys to the explosive radiation of the emerging pathogen Bartonella.";
RL PLoS Genet. 9:E1003393-E1003393(2013).
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:ENN94939.1}.
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DR EMBL; AGWD01000010; ENN94939.1; -; Genomic_DNA.
DR RefSeq; WP_010705027.1; NZ_KB915632.1.
DR AlphaFoldDB; N6URG6; -.
DR PATRIC; fig|1094502.3.peg.733; -.
DR HOGENOM; CLU_025574_0_0_5; -.
DR Proteomes; UP000014011; 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 42..66
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT SITE 245
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 369 AA; 41213 MW; EBC69463FB0275E0 CRC64;
MSNVKNGKPF KDVSNSSSNR LTDNHMFAQK RRKKSFIVRN PLVILGHFFL MMIVIIILSI
GIPLYIGKSI FEGRGMTGEE QVVLIYPGTG IREIALLLEK RGLIRSSDIF VYGVGYHQKT
THLKAGEYSI PAHASMRDIM DILVRGKSIE YTFTVPEGLT VQQVFDRLAA HEVLIGDLPK
VLPPEGSLMT DTVRFIRGTT RKEIINRLRE GQTKLIHALW AARSPNLPIK SIDEFVILAS
IVEKETGIAA ERPQVAAVFY NRLAKHMRLQ SDPTVIYGLF GGKGIPSGRA IYRSDLEKET
PYNTYKIDGL PPTAIANPGR DSLKAVAHPP SSDVLYFVAD GSGGHVFSRT LEEHNMNVRK
WRALKKAKH
//
