ID Q2L108_BORA1 Unreviewed; 339 AA.
AC Q2L108;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 79.
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 OrderedLocusNames=BAV1763 {ECO:0000313|EMBL:CAJ49372.1};
OS Bordetella avium (strain 197N).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=360910 {ECO:0000313|EMBL:CAJ49372.1, ECO:0000313|Proteomes:UP000001977};
RN [1] {ECO:0000313|EMBL:CAJ49372.1, ECO:0000313|Proteomes:UP000001977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=197N {ECO:0000313|EMBL:CAJ49372.1,
RC ECO:0000313|Proteomes:UP000001977};
RX PubMed=16885469; DOI=10.1128/JB.01927-05;
RA Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA Parkhill J., Temple L.M.;
RT "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT extensive diversity in surface structures associated with host
RT interaction.";
RL J. Bacteriol. 188:6002-6015(2006).
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}.
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DR EMBL; AM167904; CAJ49372.1; -; Genomic_DNA.
DR RefSeq; WP_012417433.1; NC_010645.1.
DR AlphaFoldDB; Q2L108; -.
DR STRING; 360910.BAV1763; -.
DR GeneID; 41393615; -.
DR KEGG; bav:BAV1763; -.
DR eggNOG; COG1559; Bacteria.
DR HOGENOM; CLU_025574_0_2_4; -.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000001977; Chromosome.
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 Reference proteome {ECO:0000313|Proteomes:UP000001977};
KW Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..339
FT /note="Endolytic murein transglycosylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004211702"
FT SITE 219
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 339 AA; 37809 MW; 7371902CB1720276 CRC64;
MKKRIAFYFL LLLLLAVLAA AGAAASAWYW AQQPIKLQAD RVDFVVDPGA TPRAIARTLN
AAGVPVWEPG FVWMARLSDM DKLIKAGGYQ AINGDSPWML LQRMARGDMS QRQITFVEGW
TYRQIRAALR ENPDVKQTLG ETSDEALMDR LGSAIKQPEG LFFPDTYVFT PGSSDYDILR
RAYEEGQRVL AATWERRDPD LPMATPYEAL IMASIIEKET GHGPERARIS GVFANRLRLG
MLLQTDPTVI YGMGDAYQGR IRRRDLQTDT PWNTYTRAGL PPTPIASAGR AALLAAVQPE
KHKFLYFVSR GNGTSEFAAN LSEHNRNVSR FILGQGQNP
//
