ID E7S9Y0_9STRE Unreviewed; 532 AA.
AC E7S9Y0;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
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:EFV99672.1};
GN Synonyms=mltG {ECO:0000256|HAMAP-Rule:MF_02065};
GN ORFNames=HMPREF9421_0866 {ECO:0000313|EMBL:EFV99672.1};
OS Streptococcus australis ATCC 700641.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=888833 {ECO:0000313|EMBL:EFV99672.1, ECO:0000313|Proteomes:UP000002814};
RN [1] {ECO:0000313|EMBL:EFV99672.1, ECO:0000313|Proteomes:UP000002814}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700641 {ECO:0000313|EMBL:EFV99672.1,
RC ECO:0000313|Proteomes:UP000002814};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
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}.
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:EFV99672.1}.
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DR EMBL; AEQR01000016; EFV99672.1; -; Genomic_DNA.
DR RefSeq; WP_006595774.1; NZ_GL636091.1.
DR AlphaFoldDB; E7S9Y0; -.
DR eggNOG; COG1559; Bacteria.
DR HOGENOM; CLU_025574_1_0_9; -.
DR Proteomes; UP000002814; 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:0016740; F:transferase activity; IEA:UniProtKB-KW.
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:UP000002814};
KW Transferase {ECO:0000313|EMBL:EFV99672.1};
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 161..184
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT REGION 45..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 404
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 532 AA; 59714 MW; 573DDA681193F05D CRC64;
MTRGVKYLTD NQQENEKLLS FKERILRDLE EANKQIVQVE KEYDLPVQEI STPENKEDET
EGSHSELVSE EPEVQEKVEI PEEVERVEVP EATEVSAIQE VAEENQEETP LPIEEPTREP
ESSSQPVAVS RKEKPISSVS RKDRDQRVQK KKKQNTIAKR IVLTVLGILF VLMVATGIFA
VTYVQSNLNA MDAKATEFVT VEIPAGSSNR EIGTILEKKG LIKNGQFFNY YTKFKNYGNF
QSGYFNLQKS MDLDTIIQKL QEQGTKTPEP PVLGKITIPE GYTIDQIAEV VSVDASSKSG
AKTPYTQEEF LKVIQDDAFI EKMVAKYPKL LATLPSKESG VRYRLEGYLF PATYGYGKDS
KMEDLVDQML AAMDQNLSAY YDTMEAKNID VNEALTLASL IEKEGATDKD RKDIASVFYN
RLNQDMPLQS NIAILYAQGQ LGKKTTLKED ATIDTNIESP YNIYKNTGLM PGPVDSPGLS
AIEAAVNPSK TDYLYFVANV ETGEVYFAKT YEEHTKNVEE HVNSKLAESS SN
//
