ID   A0A095ZK98_9FIRM        Unreviewed;       458 AA.
AC   A0A095ZK98;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KGF08924.1};
GN   ORFNames=HMPREF1635_05210 {ECO:0000313|EMBL:KGF08924.1};
OS   Clostridiales bacterium S5-A14a.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales;
OC   Eubacteriales Family XIII. Incertae Sedis.
OX   NCBI_TaxID=1230734 {ECO:0000313|EMBL:KGF08924.1, ECO:0000313|Proteomes:UP000029601};
RN   [1] {ECO:0000313|EMBL:KGF08924.1, ECO:0000313|Proteomes:UP000029601}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S5-A14a {ECO:0000313|EMBL:KGF08924.1,
RC   ECO:0000313|Proteomes:UP000029601};
RA   McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA   Sutton G., Nelson K.E.;
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
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:KGF08924.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JRNA01000016; KGF08924.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A095ZK98; -.
DR   STRING; 1230734.HMPREF1635_05210; -.
DR   OrthoDB; 9803907at2; -.
DR   Proteomes; UP000029601; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR   InterPro; IPR036565; Mur-like_cat_sf.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   InterPro; IPR013564; MurT_C.
DR   PANTHER; PTHR23135:SF7; LIPID II ISOGLUTAMINYL SYNTHASE (GLUTAMINE-HYDROLYZING) SUBUNIT MURT; 1.
DR   PANTHER; PTHR23135; MUR LIGASE FAMILY MEMBER; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   Pfam; PF08353; MurT_C; 1.
DR   SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029601}.
FT   DOMAIN          55..194
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          331..437
FT                   /note="Lipid II isoglutaminyl synthase (glutamine-
FT                   hydrolyzing) subunit MurT C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08353"
SQ   SEQUENCE   458 AA;  52466 MW;  ABB570332E11CB04 CRC64;
     MSKIRFLIAF CISKFTVILL KIFSYRGSDF PGMIAIKICP DFLKYIKKPD LIIGVTGSNG
     KTTVTNLIAD SLSMLGENIV SNKFGSNLHT GVATALLRNY KIFGGVKSNI AVIEIDERSF
     RITGKYITPN YIIITNLTRD SMMRNAHPDF ISQILTKYIP ADSKLIINAD NLSAVITSPK
     NERIYFGIKQ MSTDKQISNS IIHDVNICPI CQEELVWDYC RYSDIGSVRC PKCGFHTPEY
     NYFADHVDLE NKTISFYDNS SIILDNVKLI NDTLFNIYNQ LAVMTLLSEL GYSGKEITKC
     INNLDILHSR LKFDVFHGDM QIKTMLSKGM NGYANSRVFE YINSQERPTQ IVLMINSEEV
     ETVWSENICW IYDADFELLN FDFLDKVIMF CPRKYDYKNR LLFAGVPEDK ILLLDDYRDA
     PQHIRYIKDS SVFILHDIYN EDKADFIRKS ILSGRIGS
//