ID A3CPS4_STRSV Unreviewed; 499 AA.
AC A3CPS4;
DT 20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 20-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 91.
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=pabC {ECO:0000313|EMBL:ABN45179.1};
GN Synonyms=mltG {ECO:0000256|HAMAP-Rule:MF_02065};
GN OrderedLocusNames=SSA_1797 {ECO:0000313|EMBL:ABN45179.1};
OS Streptococcus sanguinis (strain SK36).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=388919 {ECO:0000313|EMBL:ABN45179.1, ECO:0000313|Proteomes:UP000002148};
RN [1] {ECO:0000313|EMBL:ABN45179.1, ECO:0000313|Proteomes:UP000002148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK36 {ECO:0000313|EMBL:ABN45179.1,
RC ECO:0000313|Proteomes:UP000002148};
RX PubMed=17277061; DOI=10.1128/JB.01808-06;
RA Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P.,
RA Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D.,
RA Paik S., Peterson D.L., Macrina F.L., Buck G.A.;
RT "Genome of the opportunistic pathogen Streptococcus sanguinis.";
RL J. Bacteriol. 189:3166-3175(2007).
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; CP000387; ABN45179.1; -; Genomic_DNA.
DR RefSeq; WP_011837369.1; NC_009009.1.
DR RefSeq; YP_001035729.1; NC_009009.1.
DR AlphaFoldDB; A3CPS4; -.
DR STRING; 388919.SSA_1797; -.
DR KEGG; ssa:SSA_1797; -.
DR PATRIC; fig|388919.9.peg.1704; -.
DR eggNOG; COG1559; Bacteria.
DR HOGENOM; CLU_025574_1_0_9; -.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000002148; 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 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:UP000002148};
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 124..147
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT REGION 30..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 369
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 499 AA; 54881 MW; 0D0AE49132285CB0 CRC64;
MLGIMMKEVK FLTEKSQDKE KNLSFKEQIL KDLAGEKEEQ TPSSTSQSEA DAASAKETAA
AEDFEARPAS VDVSYKVAEN EKAHPQVYGR VDEEDKKPNE VLSRANRANN TVKKKRQNTL
ARRIMTTVLL IVLLGLVVTG VVGYTYVSSA LKPVDANATE YVTVEVPEGS SSKQIGEILE
KKGLIKNAQV FSLYSKIKSF NNYQSGYYNL QKSMDLDTIA RQLQEGGTDT PQPPVVGKVT
IPEGYTLEQI AEAVTVNAAA TSKKTSKTPF SKDDFLAKVQ DEAFISKMAA KYPQLLGTLP
SKDSGVKYRL EGYLFPATYN YGEDADLESL IDQMLGAMNT NLSSYYSTIE AKNLTVNEVL
TLASLVEKEG STDQDRKDIA SVFYNRLNQA MPLQSNIAIL YAQGKLGKKT TLKEDAEIDT
NIDSPFNVYK KEGLMPGPVD SPSMSALEAT INPSKTDYLY FVANVETGAV YFANTYEEHA
KNVEEHVNSK LTQSSSSSN
//
