ID H9UM13_SPIAZ Unreviewed; 336 AA.
AC H9UM13;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=Spiaf_2526 {ECO:0000313|EMBL:AFG38556.1};
OS Spirochaeta africana (strain ATCC 700263 / DSM 8902 / Z-7692).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC Spirochaeta.
OX NCBI_TaxID=889378 {ECO:0000313|EMBL:AFG38556.1, ECO:0000313|Proteomes:UP000007383};
RN [1] {ECO:0000313|Proteomes:UP000007383}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 700263 / DSM 8902 / Z-7692
RC {ECO:0000313|Proteomes:UP000007383};
RX PubMed=23991249; DOI=10.4056/sigs.3607108;
RA Liolos K., Abt B., Scheuner C., Teshima H., Held B., Lapidus A., Nolan M.,
RA Lucas S., Deshpande S., Cheng J.F., Tapia R., Goodwin L.A., Pitluck S.,
RA Pagani I., Ivanova N., Mavromatis K., Mikhailova N., Huntemann M., Pati A.,
RA Chen A., Palaniappan K., Land M., Rohde M., Tindall B.J., Detter J.C.,
RA Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Woyke T.,
RA Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of the halophilic bacterium Spirochaeta africana
RT type strain (Z-7692(T)) from the alkaline Lake Magadi in the East African
RT Rift.";
RL Stand. Genomic Sci. 8:165-176(2013).
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 -!- SIMILARITY: Belongs to the transglycosylase MltG family.
CC {ECO:0000256|HAMAP-Rule:MF_02065}.
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DR EMBL; CP003282; AFG38556.1; -; Genomic_DNA.
DR RefSeq; WP_014456538.1; NC_017098.1.
DR AlphaFoldDB; H9UM13; -.
DR STRING; 889378.Spiaf_2526; -.
DR KEGG; sfc:Spiaf_2526; -.
DR PATRIC; fig|889378.3.peg.2502; -.
DR eggNOG; COG1559; Bacteria.
DR HOGENOM; CLU_025574_2_2_12; -.
DR Proteomes; UP000007383; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
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 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:UP000007383};
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 SITE 224
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 336 AA; 37504 MW; EE946A18DE2721D7 CRC64;
MKRLLFGCIT VLGVAVLLAI GTAFWALSGS PVSFQDDIII SIERGQGTRS ITRMLQSEGV
VRHARLTELY ARVTGTDTGL QAGRYLIPAG MPAAEIMRKI HSGDAVFEHI RVTIPEGWMI
NEIDAHLAGL GIYADGDFIR AAEDYARDPQ RFPLLAYIPP QVSIEGYLFP QTYFILAETE
PAELIDRMLA ELHRSLPADI EERAAEQGMT VHEVLTLASI VQKESPAGDK HGIAGVFWNR
LQRRIRLESD ATVNYVLGTR NLQPTFADTA VQHPYNTYRN FGLPPGPIGN PGLEAIEATL
DPDEHDYLFF LHKPTRETVF SYTFAEHLDA KRRYLD
//
