ID Q9KXQ1_STRCO Unreviewed; 582 AA.
AC Q9KXQ1;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 99.
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=SCO1499 {ECO:0000313|EMBL:CAB93379.1};
GN ORFNames=SC9C5.23c {ECO:0000313|EMBL:CAB93379.1};
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226 {ECO:0000313|EMBL:CAB93379.1, ECO:0000313|Proteomes:UP000001973};
RN [1] {ECO:0000313|EMBL:CAB93379.1, ECO:0000313|Proteomes:UP000001973}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145
RC {ECO:0000313|Proteomes:UP000001973};
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.H.,
RA Kieser T., Larke L., Murphy L., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
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 membrane {ECO:0000256|HAMAP-Rule:MF_02065};
CC Single-pass membrane protein {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; AL939109; CAB93379.1; -; Genomic_DNA.
DR RefSeq; NP_625779.1; NC_003888.3.
DR RefSeq; WP_003977327.1; NZ_VNID01000021.1.
DR AlphaFoldDB; Q9KXQ1; -.
DR STRING; 100226.gene:17759085; -.
DR PaxDb; 100226-SCO1499; -.
DR PATRIC; fig|100226.15.peg.1508; -.
DR eggNOG; COG1559; Bacteria.
DR HOGENOM; CLU_025574_4_3_11; -.
DR InParanoid; Q9KXQ1; -.
DR OrthoDB; 9814591at2; -.
DR PhylomeDB; Q9KXQ1; -.
DR Proteomes; UP000001973; 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; 3.30.1490.480; 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 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:UP000001973};
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 229..250
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT REGION 1..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 458
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 582 AA; 63706 MW; C1303771BF070F5F CRC64;
MTEYGRGPGS EPWHPEDPLY GDGGWGGQQA QAGQQSPYGG QPQQYPEQQA QQGYGDWSNG
GQASYGDGQP QYDQYAHQHP EPQYDPYGQQ QYDQHQYGQQ QYDQQYAPQA QPQQGYDNGG
WGGGAHPQAQ YPADPSDPYG QQAGGYGAEQ PDFYGTPEAY PPPEPPTRRR AEPEPQRTDW
DPGPDEGEHA FFAGGDADGD DDAPGDGRES REERRTRGGG KPKKRRSGCA CLVVCLVLGG
GVAGIGYFGY QFYQDRFGAA PDFAGGGNGE QVTVTIPKGA GGSTIGQELK RQGVVKSVDA
FISAQQSNPR GKSIQDGVYT LQKEMSAESA VELLLSPKSR SNLIIAEGRR NADVYKLIDK
RLEVKAGTTA EVAKSEYKSL GLPDWALNHK DVKDPLEGFL YPSSYSAAKG QKPADVLKQM
VARANEQYEK IGLEQKAEGL GLEGPWELLT AASLVQAEGK THEDFRKMAE VIYNRLKTDN
TETNQKLQFD STFNYLMGQS KIHISESEIN TNPDPYNTYY HRGLPPGPIS NPGEEALQAA
LNPTEEGWIY FVATDGVKKT EFAKTHDEFL KLKDKFDASS GN
//
