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Database: UniProt
Entry: A0A1S1R622_9ACTN
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Original site: A0A1S1R622_9ACTN 
ID   A0A1S1R622_9ACTN        Unreviewed;       489 AA.
AC   A0A1S1R622;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
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   ORFNames=CC117_13375 {ECO:0000313|EMBL:OHV41181.1};
OS   Parafrankia colletiae.
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae;
OC   Parafrankia.
OX   NCBI_TaxID=573497 {ECO:0000313|EMBL:OHV41181.1, ECO:0000313|Proteomes:UP000179627};
RN   [1] {ECO:0000313|Proteomes:UP000179627}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cc1.17 {ECO:0000313|Proteomes:UP000179627};
RA   Ghodhbane-Gtari F., Swanson E., Gueddou A., Morris K., Hezbri K., Ktari A.,
RA   Nouioui I., Abebe-Akele F., Simpson S., Thomas K., Gtari M., Tisa L.S.,
RA   Hurst S.;
RT   "Sequence Frankia sp. strain CcI1.17.";
RL   Submitted (JUL-2016) 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:OHV41181.1}.
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DR   EMBL; MBLM01000058; OHV41181.1; -; Genomic_DNA.
DR   RefSeq; WP_071083241.1; NZ_MBLM01000058.1.
DR   AlphaFoldDB; A0A1S1R622; -.
DR   OrthoDB; 9814591at2; -.
DR   Proteomes; UP000179627; 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: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:UP000179627};
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        145..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT   REGION          1..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          115..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..52
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            366
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ   SEQUENCE   489 AA;  51106 MW;  2D9C2A98AC7D29DE CRC64;
     MSRNGGGFDD LFGGAGYDDD RDDRRVGGRA ERHRTAATSG PGRRRQDRAG YADPGYDEAA
     YGEAGYGASS HASDDPDSDG YDPAPAGYDP VYADDAGYDG DSAYADDGGY GGGGYGDDGG
     AGRRGGRGHP EASGGRRPAR ALPKLIGVLV VVAALLGAGI FGIGKVIGRV GGEPAADYSG
     IGEGIVVVQI PAGATSSDIG TALAKADVVA SGRAFVNVAT RDSRALSIQP GTYRLRSKMS
     AASALDALLD DASSALFRYT ISPGDTVRRV LQALSARTGT PLAELEALVR DPSSLGLPDY
     AGGKLEGYLF PSTYDVAPDT DPVDVLKEAV ARFSAYADEH DIAGRARALG REPGAIVIVA
     SIIEKEVANE SEGPKVARVI YNRLADDSGR FRRLDMDSTT RYAANEHEGP LTREQLDNDD
     PYNTRAVPGL PPGAIASPSP WALESALNPA DGPWFYFVSM PQTRETVFAA NQAEFDVAMA
     EYHRQGGSE
//
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