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Entry: F6GBZ2_LACS5
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ID   F6GBZ2_LACS5            Unreviewed;       347 AA.
AC   F6GBZ2;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   24-JAN-2024, entry version 51.
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=Lacal_0007 {ECO:0000313|EMBL:AEG99859.1};
OS   Lacinutrix sp. (strain 5H-3-7-4).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Lacinutrix.
OX   NCBI_TaxID=983544 {ECO:0000313|EMBL:AEG99859.1, ECO:0000313|Proteomes:UP000008297};
RN   [1] {ECO:0000313|EMBL:AEG99859.1, ECO:0000313|Proteomes:UP000008297}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5H-3-7-4 {ECO:0000313|EMBL:AEG99859.1,
RC   ECO:0000313|Proteomes:UP000008297};
RX   PubMed=21725025; DOI=10.1128/JB.05518-11;
RA   Klippel B., Lochner A., Bruce D.C., Walston Davenport K., Detter C.,
RA   Goodwin L.A., Han J., Han S., Hauser L., Land M.L., Nolan M.,
RA   Ovchinnikova G., Pennacchio L., Pitluck S., Tapia R., Woyke T.,
RA   Wiebusch S., Basner A., Abe F., Horikoshi K., Keller M., Antranikian G.;
RT   "Complete genome sequences of Krokinobacter sp. strain 4H-3-7-5 and
RT   Lacinutrix sp. strain 5H-3-7-4, polysaccharide-degrading members of the
RT   family Flavobacteriaceae.";
RL   J. Bacteriol. 193:4545-4546(2011).
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}.
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DR   EMBL; CP002825; AEG99859.1; -; Genomic_DNA.
DR   RefSeq; WP_013868644.1; NC_015638.1.
DR   AlphaFoldDB; F6GBZ2; -.
DR   STRING; 983544.Lacal_0007; -.
DR   KEGG; lan:Lacal_0007; -.
DR   eggNOG; COG1559; Bacteria.
DR   HOGENOM; CLU_025574_2_0_10; -.
DR   OMA; AVNKYQR; -.
DR   OrthoDB; 9814591at2; -.
DR   Proteomes; UP000008297; Chromosome.
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   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:UP000008297};
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        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT   SITE            216
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ   SEQUENCE   347 AA;  39886 MW;  4D220674F252694E CRC64;
     MYIKKILVAI AIIGLAIAAY FAYFIYGAML KPNTAFNNEE AYIFIPTHAK YQEVREQLEP
     LLIDIDGFDA LAEQKKYTTN IKAGRFVIKK GMSNNDIINS IRSKNIPLRV AFNNQERLED
     LAGRIAFQIE PDSLTLLMAM TDPEFLSKNN FNEDTALAMY IPNSYEFFWN TSAEGFRDKM
     LKEYNRFWTA EREAKAKKLN LSKNEVIALA AIVHKETAKV DERPRVAGVY LNRLRKGIPL
     QADPTVIYAV KKQDGNFNRV IKRVLYKDLE TNSPYNTYKN AGVPPGPIFM PDVSAIDAVL
     NPEKHDYIYF VANVKNFGYH KFAKTLSQHN QNKQEYVRWI NKQGVNR
//
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